Hydrolysis of porcine b-casein by bovine plasmin and bovine chymosin
|
|
- Meghan Adams
- 6 years ago
- Views:
Transcription
1 Z Lebensm Unters Forsch A (1999) 208 : Q Springer-Verlag 1999 ORIGINAL PAPER Daniel P. Gallagher 7 Tanoj K. Singh Daniel M. Mulvihill Hydrolysis of porcine b-casein by bovine plasmin and bovine chymosin Received: 9 February 1998 / Revised version: 2 June 1998 Abstract The action of bovine chymosin and bovine plasmin on porcine b-casein was studied and compared with their effect on bovine b-casein in an attempt to elucidate the similarities in specificity of these enzymes on porcine and bovine b-caseins. Bovine plasmin rapidly hydrolysed porcine b-casein at Lys 106 -Arg 107, Lys 49 -Ile 50 and Lys 168 -Val 169 to yield g-caseins. Several peptides that had the same N-terminal amino acid sequence as porcine b-casein were also produced. Plasmin hydrolysis sites determined by separating the ph 4.6-soluble peptides formed on hydrolysis were Lys 33 - Leu 34, Lys 49 -Ile 50, Lys 95 -Asp 96, Lys 98 -Ala 99, Lys Arg 107, Lys 108 -Gly 109 and Lys 168 -Val 169. Porcine b-casein, like bovine b-casein, was hydrolysed by bovine chymosin into three distinct electrophoretic bands designated porcine b-i-, b-ii- and b-iii-casein, all of which had the N-terminal sequence of porcine b-casein. Two initial ph 4.6-soluble peptides formed on hydrolysis of porcine b-casein by chymosin had N-terminal amino acid sequences commencing at porcine b-casein amino acid 197, suggesting that porcine b-i-casein corresponds to fragment 1 196, while the sequences of two other small peptides commenced at amino acids 1 and 207. The C-terminal cleavage site(s) leading to formation of porcine b-ii and b-iii casein were not determined. Key words Porcine b-casein 7 Bovine b-casein 7 Hydrolysts 7 Bovine plasmin 7 Bovine chymosin Introduction D.P. Gallagher 7 T.K. Singh 7 D.M. Mulvihill (Y) Department of Food Chemistry, University College, Cork, Ireland The first report on the isolation of porcine b-casein was by Woychik and Wondolowski [1] but the protein was not characterised by them. Mulvihill and Fox [2] isolated porcine b-casein and reported that it contained 218 amino acids, had eight phosphorus residues per mole and a molecular weight of Da. Bovine b- casein contains 209 amino acids, has five phosphorus residues per mole and has a molecular weight of Da [3]. The full amino acid sequence of porcine b-casein has been derived from its cdna [4]; these authors reported that porcine b-casein contains 217 amino acid residues, has six potential phosphorylation sites and a molecular weight, in the non-phosphorylated form, of Da. In agreement with Mulvihill and Fox [2], Alexander and Beattie [4] reported that porcine b-casein contains higher levels of Ser, Ala and Leu than its bovine counterpart, but they also reported higher levels of Lys and an absence of Trp relative to bovine b-casein. Porcine and bovine b-caseins contain similar levels of hydrophobic amino acids (46 and 44%, respectively) and Pro, and both proteins are devoid of Cys. Bovine b-casein in solution is hydrolysed sequentially by bovine chymosin at bonds Leu 192 -Tyr 193, Ala Phe 190, Leu 163 -Ser 164 and Leu 139 -Leu 140 to yield the peptides b-i 1, b-i 11, b-ii and b-iii casein, respectively; bonds Leu 165 -Ser 166 and Gln 167 -Ser 168 may also be hydrolysed to yield peptides indistinguishable electrophoretically from b-ii caseins [5, 6]. Bovine b-casein is hydrolysed by plasmin at bonds Lys 28 -Lys 29, Lys His 106 and Lys 107 -Glu 108 to yield g-caseins [g 1 (b-casein f29 209), g 2 (b-casein f ) and g 3 (b-casein f )] and protease peptones (PP) [PP-5 (b-casein f1 105/107), PP-8 slow (b-casein f /107) and PP-8 fast (b-casein f1 28)] [7]. Visser et al. [8] identified sixteen peptides (1 25, 1 28, 2 25, 2 28, 29 48, 33 48, 33 97/99, 49 97, 49 99, , , , , , , ) in plasmin hydrolysates of bovine b-casein; most Lys-X and Arg-X bonds were hydrolysed. The specificity of proteolytic enzymes on porcine b- casein has received little attention. In the present study, the action of bovine chymosin and bovine plasmin on porcine b-casein was studied, and compared with the
2 84 effect of these enzymes on bovine b-casein in an attempt to elucidate the similarities in specificity of these enzymes on porcine and bovine b-caseins. Materials and methods Preparation of porcine and bovine b-casein. Bulk porcine milk (from up to four sows) was obtained from the National Dairy Products Research Centre, Moorepark, Fermoy, Co. Cork, Ireland. The sows, between 8 and 25 days post-partum, were injected intraveneously with 10 IU of oxytocin to induce milk let-down; the milk was ejected manually. The milk was defatted by centrifugation at g at 4 7C for 30 min and sodium azide (0.05%) was added as a preservative before storage at 4 7C. Bovine skim milk was obtained from the experimental creamery at University College, Cork. Porcine and bovine sodium caseinates were prepared essentially as described by Fox and Hoynes [9] except that the casein was re-dissolved and re-precipitated twice, before being dialysed against several changes of distilled water at 4 7C for 24 h, and freeze-dried. Porcine casein was fractionated essentially as described by Erhardt [10], but using a M salt gradient. A sample (0.2 g) of the caseinate was dissolved in F8 ml of 10 mm Tris-imidazole buffer, ph 7.0, containing 3.3 mol/l urea and 0.01 mol/l 2-mercaptoethanol and chromatographed on a column of DEAE-cellulose (80!2.5 cm, DEAE-52, Whatman, Maidstone, UK) which was pre-equilibrated with the same buffer. Proteins were eluted from the ion-exchanger with a linear (0 0.4 M) NaCl gradient at a flow rate of 48 ml/h and the eluate monitored at 280 nm. The fractions corresponding to b-casein were pooled and dialysed exhaustively against several changes of distilled water at 4 7C for 24 h, and freeze-dried. A sample (0.5 g) of bovine sodium caseinate was chromatographed on a column of DEAE-cellulose (90!3.5 cm, DEAE-52, Whatman) equilibrated with 10 mm imidazole buffer, ph 7.0, containing 4.5 M urea and 0.1% 2-mercaptoethanol. Proteins were eluted with a linear NaCl (0 0.5 M) gradient at a flow rate of 48 ml/h and the eluate monitored at 280 nm. The fractions corresponding to b-casein were pooled and dialysed exhaustively against several changes of distilled water at 4 7C for 24 h, and freeze-dried. Hydrolysis of porcine and bovine b-caseins with bovine chymosin and plasmin. Bovine recombinant chymosin expressed in Kluveromyces marxianus var. lactis (Maxiren) was obtained from Gist Brocades, Delft, Netherlands. Prior to use, the enzyme preparation was dialysed against two 20-volume changes of distilled water at 4 7C for 24 h and freeze-dried. The freeze-dried powder was redispersed in 100 mm potassium phosphate buffer, ph 6.5. This solution had an activity of F70 chymosin units/ml (1 unit is the activity necessary to coagulate 10 ml of bovine milk, ph 6.5, in 100 s at 30 7C). Porcine or bovine b-casein (2 mg/ml) was dissolved in 0.2 M phosphate buffer, ph 6.5, and heated to 35 7C in a water bath; chymosin was then added (0.35 units/ml), the mixture maintained at 35 7Cand samples taken periodically and chymosin inactivated by heating in boiling water for 2 min. Bovine plasmin was obtained from Sigma (St. Louis, Mo., USA). Porcine or bovine b-casein (2 mg/ml) was dissolved in 50 mm ammonium bicarbonate buffer, ph 8.4, containing 0.05% sodium azide; 0.02 units (1 unit will produce a DA 275 nm of 1.0 from a-casein in 20 min at ph 7.5 at 35 7C when measuring perchloric acid-soluble products in a volume of 5 ml) of bovine plasmin were then added per ml and the solution incubated at 35 7C. Samples were taken periodically and the plasmin inactivated by heating in a boiling water bath for 2 min. Polyacrylamide gel electrophoresis (PAGE). PAGE was performed according to the method of Andrews [11]. The gels were stained using Coomassie Brilliant Blue G-250 [12]. Reversed-phase high performance liquid chromatography (RP- HPLC). Aliquots of hydrolysate were adjusted to ph 4.6, centrifuged at g (Microcentaur centrifuge, Sanyo MSE Instruments, Leicester, UK) for 20 min. The supernatant was analysed by RP-HPLC using an automated Waters HPLC system (consisting of model 426 pump, model 600 S system controller, model 717 plus auto sampler; Millipore, Milford, Mass., USA) fitted with a Fig. 1 Urea-PAGE of porcine and bovine b-caseins following hydrolysis by bovine plasmin. Lanes 1 and 11 porcine sodium caseinate. Lanes 2 10 porcine b-casein following hydrolysis by bovine plasmin for 1, 2, 5, 10, 15, 30, 60, 120 and 180 min, respectively. The bands labelled a e were electroblotted and their N-terminal amino acid sequences determined (see Table 1). Lane 12 bovine sodium caseinate. Lanes bovine b-casein following hydrolysis by bovine plasmin for 0, 30 and 180 min, respectively
3 85 Table 1 Identity of the peptides produced from porcine b-casein by bovine plasmin at ph 8.4 Electrophoretic HPLC N-terminal sequence Mass of peptide Position in porcine band a peak no. b b-casein sequence Exp. c Theor. d a Arg-Lys-Gly-Met-Pro P 107? b Arg-Lys-Gly-Met-Pro P 107? c Ile-His-Gln-Phe-Pro P 50? d Val-Leu-Pro-Val-Pro P 169? e Arg-Ala-Lys-Glu-Glu P 1? 1 Leu-Lys-Arg-Glu-Glu Ala-Lys-Glu-Thr-Ile Asp-Ser-Lys-Ala-Lys ND f 96? 4 Arg-Ala-Lys-Glu-Glu ND f 1? 5 Ile-His-Gln-Phe-Pro ND f 50? 6 Ile-His-Gln-Phe-Pro Ile-His-Gln-Phe-Pro e Ile-His-Gln-Phe-Pro e Val-Leu-Pro-Val-Pro ND f 169? 10 Arg-Lys-Gly-Met-Pro Val-Leu-Pro-Val-Pro ND f 169? a See Fig. 1 b See Fig. 3 c Experimental d Theoretical e Mass difference is due to addition of Na c, K c P or HCO 3 f Not determined Table 2 Identity of the peptides produced from porcine b-casein by bovine chymosin at ph 6.5 Electrophoretic band a HPLC N-terminal sequence Position in porcine peak no. b b-casein sequence a Arg-Ala-Lys-Glu-Glu 1? b Arg-Ala-Lys-Glu-Glu 1? c Arg-Ala-Lys-Glu-Glu 1? 1 Gly-Phe-Tyr-Pro-Val c 207 c? 2 Tyr-Gln-Asp-Pro-Leu 197? 3 Tyr-Gln-Asp-Pro-Leu 197? 4 Tyr-Gln-Asp-Pro-Leu 197? 5 Arg-Ala-Lys-Glu-Glu 1? a See Fig. 5 b See Fig. 6 c Alexander and Beattie [4] reported Ala instead of Val at amino acid residue 211 wide-pore C 8 column (5 mm particle size, 300 Å pore size, 280!4.6 mm; HPLC Technology, Macclesfield, UK) and guard column (20!4.6 mm). A 150 ml sample was injected onto the column and eluted using a gradient of two solvents: A, 0.1% trifluoroacetic acid (TFA; sequencing grade, Sigma) in deionised water; B, 0.1% TFA in acetonitrile [HPLC (far-uv) grade, Labscan, Dublin, Ireland]. Elution was initially with 100% A for 5 min, then with a linear gradient of 0 50% B over 55 min, B was maintained at 50% for a further 6 min and then increased to 60% over 4 min, and maintained at 60% for 3 min. The eluate was monitored at 214 nm using a Waters model 486 programmable detector (Millipore) interfaced with a personal computer controlled by Millenium 2010 software (Millipore). The flow rate was maintained at 0.75 ml/min. Eluted peptides were collected manually in polypropylene tubes and freeze-dried before further analysis. Electroblotting. Protein bands were transferred from a urea- PAGE gel to a poly (vinylidene difluoride) membrane (PVDF, pore size 0.22 mm ProBlott, Applied Biosystem, Foster City, Calif., USA) using a MiniTrans-Blott electrophoretic transfer cell (Bio-Rad, San Ramon, Calif., USA). Electrophoresis was performed at 90 V for 15 min in CAPS [3-(cyclohexylamino)-1-propanesulfonic acid] transfer buffer. The PVDF membranes were then stained using 0.2% (w/v) Coomassie Blue R-250 in 1% (v/v) acetic acid for min, followed by destaining in distilled water. Individual protein bands were cut out from the membrane and sequenced directly. Peptide identification. Peptides were sequenced by an automated Edman degradation method using a pulsed-liquid phase protein/ peptide sequencer (Model 477A, Applied Biosystem). Liberated amino acids were detected as their phenylthiohydantoin derivatives by a model 120A microbore HPLC (Applied Biosystem). Mass analysis on isolated peptides was studied using a BioIon- 20 plasma desorption mass spectrometer (BioIon AB, Uppsala, Sweden). Samples were dissolved in 50% (v/v) methanol containing 1% TFA and applied to nitrocellulose-covered aluminised mylar targets. The samples were usually washed with small (F50 ml) volumes of 0.1 M ammonium bicarbonate to reduce the interference from Na c and/or K c.
4 86 Fig. 2 Primary sequence of bovine (B) [13] and porcine (P) [4] b-casein. Underlined amino acids indicate differences between the porcine and bovine proteins. Known plasmin hydrolysis sites are indicated by ( * ) while known chymosin hydrolysis sites are indicated by (c) Results and discussion Urea-PAGE (Fig. 1) showed that porcine and bovine b-caseins were hydrolysed rapidly by bovine plasmin; several electrophoretic bands migrating in the protease peptone region of the electrophoretic gel were evident in hydrolysates of both proteins. Bovine b-casein hydrolysates had three main bands in the g-casein region,
5 87 Fig. 3a, b RP-HPLC elution profile of ph 4.6-soluble peptides from porcine b-casein following hydrolysis by bovine plasmin for a 30 and b 180 min. The peptides in peaks labelled 1 11 were recovered and their N-terminal amino acid sequences and molecular weights determined (see Table 1) while the porcine b-casein hydrolysates exhibited four bands in this region. The four main porcine g-casein bands (a d) and one porcine proteose peptone band (e) were electroblotted from the electrophoretic gel and their N-terminal sequences determined (see Table 1). Porcine g-caseins a and b resulted from the cleavage of porcine b-casein at Lys 106 -Arg 107 (Fig. 2), while porcine g-caseins c and d resulted from the hydrolysis of Lys 49 -Ile 50 and Lys 168 -Val 169, respectively. Bovine g 1 - casein results from the hydrolysis of bovine b-casein at Lys 28 -Lys 29, but no similar hydrolysis site was found in porcine b-casein. Bovine g 2 - and g 3 -caseins result from the hydrolysis of Lys 105 -His 106 and Lys 107 -Glu 108, respectively. The N-terminal amino acid sequence of band e was the same as porcine b-casein, indicating that this band was a proteose peptone. Figure 3 shows the HPLC elution profile of the ph 4.6-soluble peptides formed on hydrolysis of porcine b-casein by bovine plasmin for 30 and 180 min. The peptides in peaks labelled 1 11 were isolated and their N-terminal sequences and molecular weights determined (Table 1). The main hydrolysis sites identified were Lys 33 -Leu 34, Lys 49 -Ile 50, Lys 95 -Asp 96, Lys 98 -Ala 99, Lys 106 -Arg 107, Lys 108 -Gly 109 and Lys 168 -Val 169. The plasmin hydrolysis sites in porcine b-casein and the identity of some of the peptides produced are illustrated schematically in Fig. 4. Like bovine b-casein, the N-terminal half of porcine b-casein appears to be more susceptible to hydrolysis by plasmin than the C-terminal region. Although plasmin cleaved porcine b-casein at Lys Arg 107 and Lys 108 -Gly 109, only one of these sites (Lys 106 -Arg 107 ) resulted in the production of a g-casein (Fig. 2); however, bovine g 2 - and g 3 -caseins resulted from the hydrolysis of two similar sites in bovine b- casein (i.e., Lys 105 -His 106 and Lys 107 -Glu 108 ). Urea-PAGE of porcine and bovine b-casein following hydrolysis by bovine chymosin is shown in Fig. 5. Bovine b-casein was hydrolysed to b-i, b-ii and b-iii casein over the 24-h period. Porcine b-casein was also hydrolysed to three distinct electrophoretic bands (a c) Fig. 4 Schematic of the identified sites of hydrolysis of porcine b-casein by bovine plasmin
6 88 Fig. 5 Urea-PAGE of porcine and bovine b-casein following hydrolysis by bovine chymosin. Lane 1 porcine sodium-caseinate. Lanes 2 12 porcine b- casein following hydrolysis by bovine chymosin for 0, , 1, 2, 4, 8, 10, 12, 16 or 24 h, respectively. Lanes bovine b-casein following hydrolysis by bovine chymosin for 0, 2 or 24 h, respectively. The bands labelled a, b and c were electroblotted and their N-terminal amino acid sequences determined (see Table 2) over the same time period. The first band (a) had a lower electrophoretic mobility than bovine b-i-casein, while band (b) had a higher electrophoretic mobility than bovine b-ii-casein; the electrophoretic mobility of band (c) was very similar to bovine b-iii-casein. Mulvihill and Fox [2] found that porcine b-casein was rapidly hydrolysed to b-i, which corresponded in electrophoretic mobility to bovine b-i casein, and suggested that a similar peptide bond was cleaved in both proteins. The authors stated that porcine b-i casein was further hydrolysed to a peptide doublet with a similar electrophoretic mobility to bovine b-iii casein and no peptide corresponding in mobility to bovine b-ii casein was evident in their porcine b-casein hydrolysate. The N-terminal sequence of the electrophoretic bands a, b and c (Table 2) was the same as porcine b-casein, indicating that the formation of these peptides involved hydrolysis towards the C-terminal of the protein. Figure 6 shows the resolution of the ph 4.6-soluble peptides formed from porcine b-casein by bovine chymosin over the 24-h period The peaks labelled 1 5 were isolated and their N-terminal sequences determined (Table 2). Peaks 3 and 4 were evident in chromatograms of the ph 4.6-soluble peptides formed after 2 h of hydrolysis and probably contained the small peptide(s) cleaved from porcine b-casein in the formation of band a in Fig. 5, which was the first large peptide formed from porcine b-casein. The N-terminal amino Fig. 6a, b RP-HPLC elution profile of ph 4.6-soluble peptides from porcine b-casein following hydrolysis by bovine chymosin for a 2 and b 24 h. The peptides in peaks labelled 1 5 were recovered and their N-terminal amino acid sequences determined (see Table 2)
7 89 acid sequences of peptides 2, 3 and 4 (Fig. 6) identified the hydrolysis site as Leu 196 -Tyr 197. These results suggest that porcine b-casein fragment corresponds to band a (porcine b-i-casein), as the N-terminal amino acid sequence of this electrophoretic band was the same as that of porcine b-casein. This confirms the suggestion of Mulvihill and Fox [2] that a similar bond was cleaved in both porcine and bovine b-casein to yield porcine and bovine b-i-casein. The N-terminal amino acid sequence of the ph 4.6-soluble peptide 1 (Fig. 5) suggested that porcine b-casein was also cleaved at Gln 206 -Gly 207, while the N-terminal amino acid sequence of peptide 5 corresponded to that of porcine b- casein. The electrophoretic bands b and c (Fig. 5) had the same N-terminal amino acid sequence as porcine b- casein, and it is proposed that thay be deignated porcine b-ii- and b-iii-casein, respectively; the C-terminal amino acid sequences of the peptides were not determined, and at present the complete sequences of these peptides are not known. References 1. Woychik JH, Wondolowski MV (1969) J Dairy Sci 52: Mulvihill DM, Fox PF (1979) Biochim Biophys Acta 578: Stewart AF, Bonsing J, Beattie CW, Shah F, Willis IM, MacKinlay AG (1987) Mol Biol Evol 4: Alexander LJ, Beattie CW (1992) Anim Genet 23: Pelissier JP, Mercier JC, Ribadeau-Dumas B (1974) Ann Biol Anim Biophys 14: Visser S, Slangen KJ (1977) Neth Milk Dairy J 31: Eigel WN, Butler JE, Ernstrom CA, Farrell HM, Harwalkar VR, Jenness R, Whitney R McL (1984) J Dairy Sci 67: Visser S, Slangen KJ, Alting AC, Vreeman HJ (1989) Milchwissenschaft 44: Fox PF, Hoynes MCT (1975) J Dairy Res 42: Erhardt G (1989) Milchwissenschaft 44: Andrews AT (1983) J Dairy Res 50: Blakesley RW, Boezi JA (1977) Anal Biochem 82: Swaisgood HE (1992) Chemistry of the caseins. In: Fox PF (ed) Advanced dairy chemistry-proteins, vol 1. Elsevier, Amsterdam, pp Acknowledgement Mass analysis on isolated peptides was carried out at the Department of Biochemistry, Faculty of Medicine, Nottingham University, Nottingham, UK.
Nature Methods: doi: /nmeth Supplementary Figure 1
Supplementary Figure 1 Subtiligase-catalyzed ligations with ubiquitin thioesters and 10-mer biotinylated peptides. (a) General scheme for ligations between ubiquitin thioesters and 10-mer, biotinylated
More informationAntoine Bouchoux, Pierre-Emerson Cayemitte, Julien Jardin, Geneviève Gésan-Guiziou, and Bernard Cabane
Biophysical Journal, Volume 96 Supplementary Material Casein Micelle Dispersions under Osmotic Stress Antoine Bouchoux, Pierre-Emerson Cayemitte, Julien Jardin, Geneviève Gésan-Guiziou, and Bernard Cabane
More informationBIOCHEMISTRY REVIEW. Overview of Biomolecules. Chapter 4 Protein Sequence
BIOCHEMISTRY REVIEW Overview of Biomolecules Chapter 4 Protein Sequence 2 3 4 Are You Getting It?? A molecule of hemoglobin is compared with a molecule of lysozyme. Which characteristics do they share?
More informationSUPPLEMENTARY MATERIAL
SUPPLEMENTARY MATERIAL Purification and biochemical properties of SDS-stable low molecular weight alkaline serine protease from Citrullus Colocynthis Muhammad Bashir Khan, 1,3 Hidayatullah khan, 2 Muhammad
More informationChapter PURIFICATION OF ALKALINE PROTEASES
Chapter PURIFICATION OF ALKALINE PROTEASES E /xtracellular alkaline proteases produced by Bacillus sp. K 25 and bacillus pumilus K 242, were purified and the homogeneity was examined by electrophoresis.
More informationRITONAVIRI COMPRESSI RITONAVIR TABLETS. Final text for addition to The International Pharmacopoeia (July 2012)
July 2012 RITONAVIRI COMPRESSI RITONAVIR TABLETS Final text for addition to The International Pharmacopoeia (July 2012) This monograph was adopted at the Forty-sixth WHO Expert Committee on Specifications
More informationQuantitative LC-MS/MS Analysis of Glucagon. Veniamin Lapko, Ph.D June 21, 2011
Quantitative LC-MS/MS Analysis of Glucagon Veniamin Lapko, Ph.D June 21, 2011 Contents Comparison with small molecule LC-MS/MS LC-MS/MS sensitivity of peptides detection Stability: neat vs. matrix solutions
More informationMercaptoethanesulfonic acid as the reductive thiol-containing reagent employed for the derivatization of amino acids with o-phthaldialdehyde analysis
Acta Univ. Sapientiae, Alimentaria, 1 (2008) 49 60 Mercaptoethanesulfonic acid as the reductive thiol-containing reagent employed for the derivatization of amino acids with o-phthaldialdehyde analysis
More informationHPLC '88. Poster Presentation. Isolation of Thymosin B4 from Thymosin Fraction 5 by Reverse Phase HPLC
Essentials in HPLC '88 Poster Presentation Isolation of Thymosin B4 from Thymosin Fraction 5 by Reverse Phase HPLC M. Badamchian, M.P. Strickler, M.J. Stone, A.L. Goldstein for Waters.bioresearchThe absolute,
More informationWheat Amino acids & Peptides for Hair Care. INCI Name EU/USA CAS # EINECS # Hydrolyzed wheat protein
KELYAMIN Wheat Amino acids & Peptides for Hair Care Identification INCI Name EU/USA CAS # EINECS # Hydrolyzed wheat protein 70084-87-6 305-225-0 Composition % Liquid Powder Aqua Hydrolyzed wheat protein
More informationElectronic Supplementary Information. Table of Contents
Electronic Supplementary Information Examination of native chemical ligation using peptidyl prolyl thioester Takahiro Nakamura, Akira Shigenaga, Kohei Sato, Yusuke Tsuda, Ken Sakamoto, and Akira Otaka*
More informationSupplementary material: Materials and suppliers
Supplementary material: Materials and suppliers Electrophoresis consumables including tris-glycine, acrylamide, SDS buffer and Coomassie Brilliant Blue G-2 dye (CBB) were purchased from Ameresco (Solon,
More informationTENOFOVIR TABLETS: Final text for addition to The International Pharmacopoeia (June 2010)
June 2010 TENOFOVIR TABLETS: Final text for addition to The International Pharmacopoeia (June 2010) This monograph was adopted at the Forty-fourth WHO Expert Committee on Specifications for Pharmaceutical
More informationSaccharomyces cerevisiae*
THE JOURNAL OF BIOLOGICAL CHEMISTRY 1988 by The American Society for Biochemistry and Molecular Biology, Inc. Vol. 263, No. 29, Issue of October 15, pp. 14948-14955, 1988 Printed in U.S.A. Purification
More informationIsolation, Purification and Molecular Weight Determination of Antihypertensive Peptides Derived from
2011, Vol. 32, No. 02 213 1,2 1 1, * 1 1 (1. 361012 2. 350002) AS.1398 (Porphyra haitanesis)ace Sephadex G-15 (RP-HPLC) (MALDI-TOF-MS) 2000D ACE IC50 0.73mg/mL Sephadex G-15 6 E IC50 0.67mg/mL E RP-HPLC
More informationThe Composition, Structure and Origin of Proteose-peptone Component 8F of Bovine Milk
Eur. J. Biochem. YO, 67-71 (1978) The Composition, Structure and Origin of Proteose-peptone Component 8F of Bovine Milk Anthony T. ANDREWS Chemistry Department, National Institute for Research in Dairying,
More informationTenofovir disoproxil fumarate (Tenofoviri disoproxili fumaras)
C 19 H 30 N 5 O 10 P. C 4 H 4 O 4 Relative molecular mass. 635.5. Chemical names. bis(1-methylethyl) 5-{[(1R)-2-(6-amino-9H-purin-9-yl)-1-methylethoxy]methyl}-5-oxo-2,4,6,8-tetraoxa-5-λ 5 - phosphanonanedioate
More informationAnalytical Method for 2, 4, 5-T (Targeted to Agricultural, Animal and Fishery Products)
Analytical Method for 2, 4, 5-T (Targeted to Agricultural, Animal and Fishery Products) The target compound to be determined is 2, 4, 5-T. 1. Instrument Liquid Chromatograph-tandem mass spectrometer (LC-MS/MS)
More informationSupplementary Figure-1. SDS PAGE analysis of purified designed carbonic anhydrase enzymes. M1-M4 shown in lanes 1-4, respectively, with molecular
Supplementary Figure-1. SDS PAGE analysis of purified designed carbonic anhydrase enzymes. M1-M4 shown in lanes 1-4, respectively, with molecular weight markers (M). Supplementary Figure-2. Overlay of
More informationComplex Carbohydrate Society '89. Poster Presentation
4 r? Essentials in " Complex Carbohydrate Society '89 Poster Presentation Characterization of Glycoproteins by HPLC -- Peptide Mapping and Analysis of Site Specific Glycosylation G. Vella, C. Phoebe, N.
More information2. Which of the following amino acids is most likely to be found on the outer surface of a properly folded protein?
Name: WHITE Student Number: Answer the following questions on the computer scoring sheet. 1 mark each 1. Which of the following amino acids would have the highest relative mobility R f in normal thin layer
More informationThe Composition, Structure and Origin of Proteose-peptone Component 5 of Bovine Milk
Eur. J. Biochem. 9, 59-65 (1978) The Composition, Structure and Origin of Proteose-peptone Component 5 of Bovine Milk Anthony T. ANDREWS Chemistry Department, National Institute for Research in Dairying,
More informationAnalysis of L- and D-Amino Acids Using UPLC Yuta Mutaguchi 1 and Toshihisa Ohshima 2*
Analysis of L- and D-Amino Acids Using UPLC Yuta Mutaguchi 1 and Toshihisa Ohshima 2* 1 Department of Biotechnology, Akita Prefectural University, Akita City, Japan; 2 Department of Biomedical Engineering,
More informationCYCLOSERINI CAPSULAE - CYCLOSERINE CAPSULES (AUGUST 2015)
August 2015 Document for comment 1 2 3 4 5 CYCLOSERINI CAPSULAE - CYCLOSERINE CAPSULES DRAFT PROPOSAL FOR THE INTERNATIONAL PHARMACOPOEIA (AUGUST 2015) DRAFT FOR COMMENT 6 Should you have any comments
More informationApplication Note. Determination of Amino acids by UHPLC with automated OPA- Derivatization by the Autosampler. Summary. Fig. 1.
Application Note Determination of Amino acids by UHPLC with automated PA- Derivatization by the Autosampler Category Bio Analysis Matrix - Method UHPLC Keywords Proteinogenic Amino acids, Canonical Amino
More informationHeparin Sodium ヘパリンナトリウム
Heparin Sodium ヘパリンナトリウム Add the following next to Description: Identification Dissolve 1 mg each of Heparin Sodium and Heparin Sodium Reference Standard for physicochemical test in 1 ml of water, and
More informationCharacterization of Disulfide Linkages in Proteins by 193 nm Ultraviolet Photodissociation (UVPD) Mass Spectrometry. Supporting Information
Characterization of Disulfide Linkages in Proteins by 193 nm Ultraviolet Photodissociation (UVPD) Mass Spectrometry M. Montana Quick, Christopher M. Crittenden, Jake A. Rosenberg, and Jennifer S. Brodbelt
More informationComplete Amino Acid Sequence of the Protease Inhibitor BWI-4a from Buckwheat Seeds
Biochemistry (Moscow), Vol. 65, No. 10, 2000, pp. 1140-1144. Translated from Biokhimiya, Vol. 65, No. 10, 2000, pp. 1347-1352. Original Russian Text Copyright 2000 by Belozersky, Dunaevsky, Musolyamov,
More informationFig.S1 ESI-MS spectrum of reaction of ApA and THPTb after 16 h.
Electronic Supplementary Material (ESI) for RSC Advances. This journal is The Royal Society of Chemistry 2014 Experiment Cleavage of dinucleotides Dinucleotides (ApA, CpC, GpG, UpU) were purchased from
More informationAvailable online at ScienceDirect. IERI Procedia 5 (2013 )
Available online at www.sciencedirect.com ScienceDirect IERI Procedia 5 (213 ) 351 356 213 International Conference on Agricultural and Natural Resources Engineering Pre-column Derivatization RP-HPLC Determination
More informationPTM Discovery Method for Automated Identification and Sequencing of Phosphopeptides Using the Q TRAP LC/MS/MS System
Application Note LC/MS PTM Discovery Method for Automated Identification and Sequencing of Phosphopeptides Using the Q TRAP LC/MS/MS System Purpose This application note describes an automated workflow
More informationEdman Sample Preparation Part 2. Bill Henzel Genentech Inc.
Edman Sample Preparation Part 2 Bill Henzel Genentech Inc. Determining a Protein is Blocked Estimate the amount of protein applied to the protein sequencer. Compare the staining intensity of the band of
More informationEASI-EXTRACT BIOTIN Product Code: P82 / P82B
EASI-EXTRACT BIOTIN Product Code: P82 / P82B Immunoaffinity columns for use in conjunction with HPLC or LC-MS/MS. For in vitro use only. AOAC Official First Action Method 2016.02 P82/V8/23.03.17 www.r-biopharm.com
More informationCHAPTER 21: Amino Acids, Proteins, & Enzymes. General, Organic, & Biological Chemistry Janice Gorzynski Smith
CHAPTER 21: Amino Acids, Proteins, & Enzymes General, Organic, & Biological Chemistry Janice Gorzynski Smith CHAPTER 21: Amino Acids, Proteins, Enzymes Learning Objectives: q The 20 common, naturally occurring
More informationSYNOPSIS STUDIES ON THE PREPARATION AND CHARACTERISATION OF PROTEIN HYDROLYSATES FROM GROUNDNUT AND SOYBEAN ISOLATES
1 SYNOPSIS STUDIES ON THE PREPARATION AND CHARACTERISATION OF PROTEIN HYDROLYSATES FROM GROUNDNUT AND SOYBEAN ISOLATES Proteins are important in food processing and food product development, as they are
More informationDELFIA Tb-DTPA ITC Chelate & Terbium Standard
AD0035P-2 (en) 1 DELFIA Tb-DTPA ITC Chelate & AD0029 Terbium Standard For Research Use Only INTRODUCTION DELFIA Tb-DTPA ITC Chelate is optimized for the terbium labelling of proteins and peptides for use
More informationAA s are the building blocks of proteins
Chamras Chemistry 106 Lecture otes Chapter 24: Amino Acids, Peptides, and Proteins General Formula: () n (') α-amino Acids: (n = 1) Example: Amino Acids and Proteins: Glycine Alanine Valine AA s are the
More informationSupporting Information
Supporting Information Cyclic Peptidyl Inhibitors against Human Peptidyl-Prolyl Isomerase Pin1 Tao Liu, Yu Liu, Hung-Ying Kao, *,, and Dehua Pei Table of Contents: Table S1. Structures of amino acid building
More information130327SCH4U_biochem April 09, 2013
Option B: B1.1 ENERGY Human Biochemistry If more energy is taken in from food than is used up, weight gain will follow. Similarly if more energy is used than we supply our body with, weight loss will occur.
More information2. Ionization Sources 3. Mass Analyzers 4. Tandem Mass Spectrometry
Dr. Sanjeeva Srivastava 1. Fundamental of Mass Spectrometry Role of MS and basic concepts 2. Ionization Sources 3. Mass Analyzers 4. Tandem Mass Spectrometry 2 1 MS basic concepts Mass spectrometry - technique
More informationBabyBio IMAC columns DATA SHEET DS
BabyBio IMAC columns DATA SHEET DS 45 655 010 BabyBio columns for Immobilized Metal Ion Affinity Chromatography (IMAC) are ready-to-use for quick and easy purification of polyhistidine-tagged (His-tagged)
More informationTitle Revision n date
A. THIN LAYER CHROMATOGRAPHIC TECHNIQUE (TLC) 1. SCOPE The method describes the identification of hydrocortisone acetate, dexamethasone, betamethasone, betamethasone 17-valerate and triamcinolone acetonide
More informationDETERMINATION OF D-AMINO ACIDS. I. HYDROLYSIS OF DNP-L- AMINO ACID METHYL ESTERS WITH CARBOXYPEPTIDASE-Y
Carlsberg Res. Commun. Vol. 49, p. 585-590, 1984 DETERMINATION OF D-AMINO ACIDS. I. HYDROLYSIS OF DNP-L- AMINO ACID METHYL ESTERS WITH CARBOXYPEPTIDASE-Y by PETER MARFEY" and MARTIN OTTESEN Department
More informationTrypsin Mass Spectrometry Grade
058PR-03 G-Biosciences 1-800-628-7730 1-314-991-6034 technical@gbiosciences.com A Geno Technology, Inc. (USA) brand name Trypsin Mass Spectrometry Grade A Chemically Modified, TPCK treated, Affinity Purified
More informationCaution: For Laboratory Use. A product for research purposes only. Eu-W1284 Iodoacetamido Chelate & Europium Standard. Product Number: AD0014
TECHNICAL DATA SHEET Lance Caution: For Laboratory Use. A product for research purposes only. Eu-W1284 Iodoacetamido Chelate & Europium Standard Product Number: AD0014 INTRODUCTION: Iodoacetamido-activated
More informationCommunication. Identification of Methionine N -Acetyltransferase from Saccharomyces cerevisiae
Communication THE JOURNAL OP BIOLOGICAL CHEMISTRY Vol. 265, No. 7, Issue of March 5, pp. 3603-3606,lSSO 0 1990 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U. S. A. Identification
More informationCaution: For Laboratory Use. A product for research purposes only. Eu-W1024 ITC Chelate & Europium Standard. Product Number: AD0013
TECHNICAL DATA SHEET Lance Caution: For Laboratory Use. A product for research purposes only. Eu-W1024 ITC Chelate & Europium Standard Product Number: AD0013 INTRODUCTION: Fluorescent isothiocyanato-activated
More informationArginine side chain interactions and the role of arginine as a mobile charge carrier in voltage sensitive ion channels. Supplementary Information
Arginine side chain interactions and the role of arginine as a mobile charge carrier in voltage sensitive ion channels Craig T. Armstrong, Philip E. Mason, J. L. Ross Anderson and Christopher E. Dempsey
More informationCan we learn something new about peptide separations after 40 years of RP and HILIC chromatography? Martin Gilar April 12, MASSEP 2016
Can we learn something new about peptide separations after 40 years of RP and HILIC chromatography? Martin Gilar April 12, MASSEP 2016 2015 Waters Corporation 1 Overview 1. 2D RP RP LC of peptides 2. RP-LC
More informationCHAPTER INTRODUCTION OF DOSAGE FORM AND LITERATURE REVIEW
132 CHAPTER 6 DEVELOPMENT AND VALIDATION OF A STABILITY-INDICATING RP-HPLC METHOD FOR SIMULTANEOUS DETERMINATION OF PARACETAMOL, TRAMADOL HYDROCHLORIDE AND DOMPERIDONE IN A COMBINED DOSAGE FORM 6.1 INTRODUCTION
More informationProteins. Amino acids, structure and function. The Nobel Prize in Chemistry 2012 Robert J. Lefkowitz Brian K. Kobilka
Proteins Amino acids, structure and function The Nobel Prize in Chemistry 2012 Robert J. Lefkowitz Brian K. Kobilka O O HO N N HN OH Ser65-Tyr66-Gly67 The Nobel prize in chemistry 2008 Osamu Shimomura,
More informationEASI-EXTRACT FOLIC ACID Product Code: P81 / P81B
EASI-EXTRACT FOLIC ACID Product Code: P81 / P81B Immunoaffinity columns for use in conjunction with HPLC or LC-MS/MS. For in vitro use only. P81/V16/13.04.15 www.r-biopharm.com Contents Page Test Principle...3
More informationWhat is most limiting?
The Amino Acid Content of Rumen Microbes, Feed, Milk and Tissue after Multiple Hydrolysis Times and Implications for the CNCPS M. E. Van Amburgh, A. F. Ortega, S. W. Fessenden, D. A. Ross, and P. A. LaPierre
More informationLANCE Eu-W1024 ITC Chelate & Europium Standard AD0013 Development grade
AD0017P-4 (en) 1 LANCE Eu-W1024 ITC Chelate & Europium Standard AD0013 Development grade INTRODUCTION Fluorescent isothiocyanato-activated (ITC-activated) Eu-W1024 chelate is optimized for labelling proteins
More informationThis exam consists of two parts. Part I is multiple choice. Each of these 25 questions is worth 2 points.
MBB 407/511 Molecular Biology and Biochemistry First Examination - October 1, 2002 Name Social Security Number This exam consists of two parts. Part I is multiple choice. Each of these 25 questions is
More informationComparison of a UPLC Method across Multiple UHPLC Systems
Comparison of a UPLC Method across Multiple UHPLC Systems Tanya Jenkins Waters Corporation, Milford, MA, U.S. INTRODUCTION In 2004, Waters introduced the ACQUITY UPLC System. Since this launch, many liquid
More informationARTENIMOLUM ARTENIMOL. Adopted revised text for addition to The International Pharmacopoeia
February 2012 ARTENIMOLUM ARTENIMOL Adopted revised text for addition to The International Pharmacopoeia This monograph was adopted at the Forty-sixth WHO Expert Committee on Specifications for Pharmaceutical
More informationIdentification of free amino acids in several crude extracts of two legumes
1 2 Identification of free amino acids in several crude extracts of two legumes using Thin Layer Chromatography 3 Authors 4 5 6 7 8 9 Taghread Hudaib Key words 10 11 12 13 14 15 16 17 18 19 20 Amino acids;
More informationAnalysis of Amino Acids Derived Online Using an Agilent AdvanceBio AAA Column
Application Note Pharmaceutical and Food Testing Analysis of Amino Acids Derived Online Using an Agilent AdvanceBio AAA Column Author Lu Yufei Agilent Technologies, Inc. Abstract A liquid chromatographic
More informationDELFIA Tb-N1 DTA Chelate & Terbium Standard
AD0029P-1 (en) 1 DELFIA Tb-N1 DTA Chelate & AD0012 Terbium Standard For Research Use Only INTRODUCTION DELFIA Tb-N1 DTA Chelate is optimized for the terbium labeling of proteins and peptides for use in
More informationINVESTIGATION OF THE PROTEIN FRACTIONS IN GOAT MILK WITH RP-HPLC TO OPTIMALIZE THE MILK PROCESSING
ANALELE UNIVERSITATII DIN ORADEA, Fascicula Ecotoxicologie, Zootehnie si Tehnologii de Industrie Alimentara INVESTIGATION OF THE PROTEIN FRACTIONS IN GOAT MILK WITH RP-HPLC TO OPTIMALIZE THE MILK PROCESSING
More informationAn Introduction to the Use of itraq Reagents for Amino Acid Analysis
An Introduction to the Use of itraq Reagents for Amino Acid Analysis Lisa Sapp Clinical Research and Forensic Toxicology Product Manager Mass Spectrometry Systems Amino Acid Analysis Using itraq Reagents
More informationantigen Y. Kajita, D. Morgan, A.B. Parkes and B. Rees Smith
Volume 87, number 2 FEBS 2756 August 985 Labelling and immunoprecipitation antigen of thyroid microsomal Y. Kajita, D. Morgan, A.B. Parkes and B. Rees Smith Endocrine Immunology Unit, 7th Floor Medicine.
More informationKey Words. Natural products Weed control
J Plant Growth Regul (1996) 15:13-17 Bioactivity of a Pentapeptide Isolated from Corn Gluten Hydrolysate on Lolium perenne L. D. L. Liu and N. E. Christians* Department of Horticulture, Iowa State University,
More informationGraham O Neill School of Agriculture, Food Science and Veterinary Medicine, UCD Dublin, Belfield, Dublin 4, Ireland Food For Health Ireland
Graham O Neill School of Agriculture, Food Science and Veterinary Medicine, UCD Dublin, Belfield, Dublin 4, Ireland Food For Health Ireland Encapsulation of amino acids and peptides to target their delivery
More informationVaTx1 VaTx2 VaTx3. VaTx min Retention Time (min) Retention Time (min)
a Absorbance (mau) 5 2 5 3 4 5 6 7 8 9 6 2 3 4 5 6 VaTx2 High Ca 2+ Low Ca 2+ b 38.2 min Absorbance (mau) 3 2 3 4 5 3 2 VaTx2 39.3 min 3 4 5 3 2 4. min 3 4 5 Supplementary Figure. Toxin Purification For
More informationOrganic Chemistry 3540
rganic Chemistry 3540 December 8, 2004 (8 Pages, 13 Parts) ame 1. (8%) Many organic compounds found in living systems are complex molecules which can be characterized, in part, by simply listing the chemical
More informationAZO-XYLAN (BIRCHWOOD)
ASSAY OF endo-1,4-ß-xylanase using AZO-XYLAN (BIRCHWOOD) S-AXBP S-AXBL 10/07 Megazyme International Ireland 2007 PRINCIPLE: This assay procedure is specific for endo-1,4-ß-d-xylanase activity. On incubation
More informationTivadar Orban, Beata Jastrzebska, Sayan Gupta, Benlian Wang, Masaru Miyagi, Mark R. Chance, and Krzysztof Palczewski
Structure, Volume Supplemental Information Conformational Dynamics of Activation for the Pentameric Complex of Dimeric G Protein-Coupled Receptor and Heterotrimeric G Protein Tivadar Orban, Beata Jastrzebska,
More informationPurification of Glucagon3 Interleukin-2 Fusion Protein Derived from E. coli
Purification of Glucagon3 Interleukin-2 Fusion Protein Derived from E. coli Hye Soon Won Dept. of Chem. Eng. Chungnam National University INTRODUCTION Human interleukin-2(hil-2) - known as T Cell Growth
More informationNote. Simplified protein hydrolysis with methanesulphonic acid at elevated temperature for the complete amino acid analysis of proteins
Journal of Chromatography, 448 (1988) 404-410 Elsevier Science Publishers B.V., Amsterdam - Printed in The Netherlands CHROM. 20 688 Note Simplified protein hydrolysis with methanesulphonic acid at elevated
More informationApplication Note. Introduction. Analysis of Total Aflatoxins in Food by HPLC and UHPLC
Introduction Aflatoxins are a group of mycotoxins produced by microorganisms such as Aspergillus flavus, Aspergillus parasiticus and Aspergillus nomius living in tropical or subtropical regions and have
More informationTyr. Gly Cys. Pro. Pro Glu. Ala. Arg. Leu. Arg. Cys. Gly. Asn. Phe. Arg. Ser Met. Cys. Lys Gly. Phe 30. Thr. Ala. Asp Phe.
Thr 1 Glu Lys Leu 14 5 Asp Lys Asn 38 55 Thr Asn 58 Lys Ile Ser Met Ile 51 Val Glu Asp Leu 30 Gln Thr Lys Asn STABILITY / STORAGE AS SUPPLIED: If stored at 2-8 C products A1153, A4529 and A3428 have a
More informationPNGase F Instruction Manual
PNGase F Instruction Manual Catalog Number 170-6883 Bio-Rad Laboratories, 2000 Alfred Nobel Dr., Hercules, CA 94547 4006094 Rev A Table of Contents Section 1 Introduction...1 Section 2 Kit Components and
More informationDRAFT MONOGRAPH FOR THE INTERNATIONAL PHARMACOPOEIA EFAVIRENZ, EMTRICITABINE AND TENOFOVIR TABLETS
September 2010 RESTRICTED DRAFT MONOGRAPH FOR THE INTERNATIONAL PHARMACOPOEIA EFAVIRENZ, EMTRICITABINE AND TENOFOVIR TABLETS (August 2010) DRAFT FOR COMMENT This document was provided by a quality control
More informationAuthors. Abstract. Introduction. Food
Improved and Simplified Liquid Chromatography/Atmospheric Pressure Chemical Ionization Mass Spectrometry Method for the Analysis of Underivatized Free Ao Acids in Various Foods Application Food Authors
More informationDetection of Low Level of Chloramphenicol in Milk and Honey with MIP SPE and LC-MS-MS
Detection of Low Level of Chloramphenicol in Milk and Honey with MIP SPE and LC-MS-MS Olga Shimelis, An Trinh, and Michael Ye Supelco, Div. of Sigma-Aldrich, Bellefonte, PA T407125 Introduction Molecularly
More informationProteomics Grade. Protocol. Catalog # Agilent Technologies. Research Use Only. Not for use in Diagnostic Procedures. Version A, January 2010
Proteomics Grade Trypsin Catalog #204310 Protocol Version A, January 2010 Research Use Only. Not for use in Diagnostic Procedures. Agilent Technologies Notices Agilent Technologies, Inc. 2010 No part of
More informationCHAPTER INTRODUCTION OF DOSAGE FORM AND LITERATURE REVIEW
51 CHAPTER 2 SIMULTANEOUS ESTIMATION OF PIOGLITAZONE, GLIMEPIRIDE AND GLIMEPIRIDE IMPURITIES IN COMBINATION DRUG PRODUCT BY A VALIDATED STABILITY-INDICATING RP-HPLC METHOD 2.1 INTRODUCTION OF DOSAGE FORM
More informationCS612 - Algorithms in Bioinformatics
Spring 2016 Protein Structure February 7, 2016 Introduction to Protein Structure A protein is a linear chain of organic molecular building blocks called amino acids. Introduction to Protein Structure Amine
More informationPROTEINS. Building blocks, structure and function. Aim: You will have a clear picture of protein construction and their general properties
PROTEINS Building blocks, structure and function Aim: You will have a clear picture of protein construction and their general properties Reading materials: Compendium in Biochemistry, page 13-49. Microbiology,
More informationDELFIA Eu-DTPA ITC Chelate & Europium Standard
AD0026P-3 (en) 1 DELFIA Eu-DTPA ITC Chelate & AD0021 Europium Standard For Research Use Only INTRODUCTION DELFIA Eu-DTPA ITC Chelate is optimized for the europium labelling of proteins and peptides for
More informationThe high efficiency of sub-2 µm UHPLC columns combined with the low pressure and high speed of monolith columns.
The high efficiency of sub-2 µm UHPLC columns combined with the low pressure and high speed of monolith columns. Fast High peak capacity Low back pressure PROTEIN PEPTIDE UHPLC COLUMNS Put these new, high-performance
More informationARABINAN
www.megazyme.com ARABINAN ASSAY PROCEDURE K-ARAB 08/18 (100 Assays per Kit) Megazyme 2018 INTRODUCTION: In the processing of apples and pears, the yield of juice can be dramatically improved by using enzymes
More informationAutomated Sample Preparation/Concentration of Biological Samples Prior to Analysis via MALDI-TOF Mass Spectroscopy Application Note 222
Automated Sample Preparation/Concentration of Biological Samples Prior to Analysis via MALDI-TOF Mass Spectroscopy Application Note 222 Joan Stevens, Ph.D.; Luke Roenneburg; Tim Hegeman; Kevin Fawcett
More informationLevel and activity of D-amino acids in mouse brain tissue and blood
1 2 3 4 5 6 7 8 9 10 11 12 13 14 SUPPLEMENTARY INFORMATION Level and activity of D-amino acids in mouse brain tissue and blood Choyce A. Weatherly 1, Siqi Du 1, Curran Parpia 1, Polan T. Santos 2, Adam
More informationEuropium Labeling Kit
Europium Labeling Kit Catalog Number KA2096 100ug *1 Version: 03 Intended for research use only www.abnova.com Table of Contents Introduction... 3 Intended Use... 3 Background... 3 Principle of the Assay...
More informationBeta Amyloid Peptides
Beta Amyloid Peptides The Most Comprehensive Collection for Alzheimer s Disease Academic Services Pharmaceutical Services Beta Amyloid Peptides The Most Comprehensive Collection for Alzheimer s Disease
More informationSupporting information
Electronic Supplementary Material (ESI) for ChemComm. This journal is The Royal Society of Chemistry 2014 Supporting information Glycan Reductive Isotope-coded Amino Acid Labeling (GRIAL) for Mass Spectrometry-based
More informationImprove Protein Analysis with the New, Mass Spectrometry- Compatible ProteasMAX Surfactant
Improve Protein Analysis with the New, Mass Spectrometry- Compatible Surfactant ABSTRACT Incomplete solubilization and digestion and poor peptide recovery are frequent limitations in protein sample preparation
More informationAmino acids-incorporated nanoflowers with an
Amino acids-incorporated nanoflowers with an intrinsic peroxidase-like activity Zhuo-Fu Wu 1,2,+, Zhi Wang 1,+, Ye Zhang 3, Ya-Li Ma 3, Cheng-Yan He 4, Heng Li 1, Lei Chen 1, Qi-Sheng Huo 3, Lei Wang 1,*
More informationAnalysis of free amino acids in tobacco with a new LC/MS/MS. procedure. S. C. Moldoveanu R.J. Reynolds Tobacco Co.
Analysis of free amino acids in tobacco with a new LC/MS/MS procedure S. C. Moldoveanu R.J. Reynolds Tobacco Co. Jeff Zhu Eurofins Background A considerable number of analytical methods are reported in
More informationEnzymes for Flavour Development in Dairy Substrates. Presented by: Blanca Camarasa Senior Business Manager
Enzymes for Flavour Development in Dairy Substrates Presented by: Blanca Camarasa Senior Business Manager Cheese composition Cheese consists of proteins and fat from milk, usually the milk of cows, goat,
More informationBiomolecules: amino acids
Biomolecules: amino acids Amino acids Amino acids are the building blocks of proteins They are also part of hormones, neurotransmitters and metabolic intermediates There are 20 different amino acids in
More information1. to understand how proteins find their destination in prokaryotic and eukaryotic cells 2. to know how proteins are bio-recycled
Protein Targeting Objectives 1. to understand how proteins find their destination in prokaryotic and eukaryotic cells 2. to know how proteins are bio-recycled As a protein is being synthesized, decisions
More information2D-LC as an Automated Desalting Tool for MSD Analysis
2D-LC as an Automated Desalting Tool for MSD Analysis Direct Mass Selective Detection of a Pharmaceutical Peptide from an MS-Incompatible USP Method Application Note Biologics and Biosimilars Author Sonja
More informationSolid-phase extraction of dissolved organic matter (SPE-DOM) from river, estuarine and open ocean waters
Solid-phase extraction of dissolved organic matter (SPE-DOM) from river, estuarine and open ocean waters Gerhard Kattner 1, Thorsten Dittmar 2, Boris Koch 1, and Norbert Hertkorn 3 1 Alfred Wegener Institute
More informationAZO-WHEAT ARABINOXYLAN
www.megazyme.com ASSAY OF endo-1,4-b-xylanase using AZO-WHEAT ARABINOXYLAN S-AWAXP S-AWAXL 05/17 Megazyme 2017 PRINCIPLE: This assay procedure is specific for endo-1,4-β-d-xylanase activity. On incubation
More informationPosterREPRINT A NOVEL APPROACH TO MALDI-TOF-MS SAMPLE PREPARATION. Presented at ABRF 2002, Austin, Texas, USA, 9th - 12th March 2002.
Introduction A NOVEL APPROACH TO MALDI-TOF-MS SAMPLE PREPARATION Ed Bouvier 2, Jeff Brown 1, Emmanuelle Claude 1, John L. Gebler 2, Weibin Chen 2, *Dominic Gostick 1, Kevin Howes 1, James Langridge 1,
More informationLocalization of Methylated Arginine in the Al Protein from Myelin
Proc. Nat. Acad. Sci. USA Vol. 68, No. 4, pp. 765-769, April 1971 Localization of Methylated Arginine in the Al Protein from Myelin STEVEN BROSTOFF AND E. H. EYLAR The Salk Institute, San Diego, California
More information