Branched Chain Amino Acid Aminotransferase of Pseudomonas
|
|
- Edwin Martin
- 5 years ago
- Views:
Transcription
1 Agric. Biol. Chem., 41 (7), 1171 `1177, 1977 Branched Chain Amino Acid Aminotransferase of Pseudomonas Yuji KOIDE, Mamoru HONMA and Tokuji SHIMOMURA Department of Agricultural Chemistry, Faculty of Agriculture, Hokkaido University, Sapporo, Japan Received December 20, 1976 sp. Branched chain amino acid aminotransferase was partially purified from Pseudomonas sp. by ammonium sulfate fractionation, aminohexyl-agarose and Bio-Gel A-0.5 m column chro matography. This enzyme showed different substrate specificity from those of other origins, namely lower reactivity for L-isoleucine and higher reactivity for L-methionine. Km values at ph 8.0 were calculated to be 0.3 mm for L-leucine, 0.3 mm for a-ketoglutarate, 1.1 mm for a-ketoisocaproate and 3.2 mm for L-glutamate. This enzyme was activated with ƒà-mercaptoethanol, and this activated enzyme had dif ferent kinetic properties from unactivated enzyme, namely, Km values at ph 8.0 were calculated to be 1.2 mm for L-leucine, 0.3 mm for a-ketoglutarate. Isocaproic acid which is the substrate analog of L-leucine was competitive inhibitor for pyridoxal form of unactivated and activated enzymes, and inhibitor constants were estimated to be 6 mm and 14 mm, respectively. In the previous paper,1) four L-alanine-aketo acid aminotransferases were separated from Pseudomonas sp. (a-aminoisobutyrate utilizing bacteria), and substrate specificity was examined for each enzyme. These re sults suggested that one of them would be branched chain amino acid-a-ketoglutarate aminotransferase (EC ). It has been known that this enzyme exists in organisms widely, especially animal en zyme has been studied in detail by Ichihara2 `6) and Taylor and Jenkins.7 `9) However, the enzymes of microorganism have not been purified and studied in detail except for Salmonella typhimurium,10) Pseudomonas aeru ginosa,l1) Neurospora crassal2) and Escherichia coli.13,14) Then, this paper presents the purification and some properties of the purified branched chain amino acid aminotransferase from Pseudomonas sp. MATERIALS AND METHODS Preparation of cell free extract. Cultivation of Pseudomonas sp. and preparation of cell free extract were described in the previous paper.1) Enzyme assay. Branched chain amino acid-aketoglutarate aminotransferase was assayed by the forward reaction with mixture containing 8 ƒêmoles of L-leucine, 4,umoles of a-ketoglutarate (a-kg), 40 ƒêmoles of potassium phosphate buffer (ph 8.0) 0.04ƒÊmole of pyridoxal 5'-phosphate and enzyme in the final volume of 0.4ml. The reaction was per formed at 30 Ž and terminated with 0.1 ml of 1.5 N HCl. Produced a-ketoisocaproate (a-kic) was measured by the method of Coleman.10) One unit of the enzyme activity represents the amount of enzyme forming I ƒêmole of a-kic per min at 30 Ž. Protein concentration was measured by micro-biuret method.15) For kinetic analysis, the reaction was carried out in 2.8 ml of mixture containing 280 moles of potassium phosphate buffer (ph 8.0), 0.28 ƒêmole of pyridoxal 5'-phosphate, varied concentrations of substrates and the enzyme at 30 Ž, and terminated by the addition of 0.2 ml of 3 N HCl. The determination of a-kic was made according to the method of Taylor and Jenkins16) except that 0.1 % dinitrophenylhydrazine solution was used. Amino acids formed in the reaction mixture were determined by the method of Tochikura.17 The reaction mixture of 0.4 ml contained 0.04 ƒêmole of pyridoxal 5'-phosphate and various amounts of L- amino and a-keto acids in 0.1 M potassium phosphate buffer (ph 8.0). The reaction was terminated with 0.1 ml of 1.5 N HCl, and 20 Id or 40 ƒêl aliquots were used to the assay. The amino acids were separated by paper chromatography using Toyo filter paper No. 50
2 1172 Y. KOIDE, M. HONMA and T. SHIMOMURA and the following solvent system: n-butanol-acetic acid-water (4-1-1) or phenol-water (3-1). For the separation of L-leucine and L-isoleucine 2-methylpro pan-2-ol-methyl ethyl ketone-28 % ammonia-water ( ) was used.18) Preparation of aminohexyl-agarose. Aminohexyl - agarose was prepared by the method of Shaltiel.19) RESULTS Purification procedure All operations were performed at 0 `5 Ž in the presence of 0.01 % ƒà-mercaptoethanol. Step 1. Ammonium sulfate fractionation (30 `60%) was carried out according to the method previously described.1) Step 2. Dialyzed enzyme solution was applied to an aminohexyl-agarose column (3.0 ~9.0 cm) which was equilibrated with 0.01 M potassium phosphate buffer (ph 7.5), and eluted with KCl linear gradient in the range of 0 to 0.6 M. The elution pattern is shown in Fig. 1. Step 3. Active fractions were concen trated, and applied to a Bio-Gel A-0.5 m column, and eluted with 0.05M potassium phosphate buffer (ph 7.5). The results of partial purification are shown in Table I. By using aminohexyl-agarose, branched chain amino acid aminotransferase was completely separated from L-tryptophan-a-KIC aminotransferase20) which was not clearly separated with other chromatographic techniques; DEAE-Sephadex A-50, DEAE-cellulose or gel filtrations. At this point, although this finally prepared enzyme was not completely pure, it was used for the following experi ments. Substrate specificity Amino donor specificity with a-kg as amino acceptor is shown in Table II. This enzyme showed high activity on L-leucine, L-methionine and L-valine, and low activity on L-isoleucine. Amino acceptor specificity with several L-amino acids is shown in Table III. Although this enzyme catalyzed transamination from branched chain amino acids to related a-keto acid analogs, a-kg was the best amino ac ceptor. FIG. 1. Chromatography of Branched Chain Amino Acid Aminotransferase on Aminohexyl-agarose. Column size, 3 ~9 cm; buffer, 0.01 M potassium pho sphate (ph 7.5); elution, 0 `0.6 M KCl linear gradi ent; \, absorbance at 280 rim; \, L-leucine-a- KG transaminase activity; œ \ œ, L-tryptophan-a- KIC transaminase activity; ~ \ ~, KCI concentration. Michaelis constants of the enzyme In the forward reaction at ph 8.0, Kin values were calculated to be 0.3 mm for both L-leucine and a-kg (Fig. 2) with the method of Velick and Vavra.21) In the reverse reaction, higher concentra tion of a-kic caused substrate inhibition (Fig. 3). Because that the enzyme assay is TABLE I. PURIFICATION PROCEDURE OF BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE
3 Branched Chain Amino Acid Aminotransferase of Pseudomonas sp FIG. 2. Double Reciprocal Plot of Initial Velocities against L-Leucine Concentration at Series of Fixed Concentrations of a-kg. The experiments were carried out in 2.8 ml reaction mixture as described in the text. TABLE II. AMINO DONOR SPECIFICITY WITH a-kg The concentrations of amino donor and a-kg are 10 mm. FIG. 3. Substrate Inhibition of a-kic at the Con stant Concentration of L-Glutamate. The reaction mixture of 0.4 ml contained 0.04 Đmole of pyridoxal 5'-phosphate, I Đmole of L-glutamate and various amounts of a-kic in 0.1 M potassium phosphate buffer (ph 8.0). based on paper chromatography,17) it is difficult to calculate Km values of a-kic and L-glutamate at lower region of concentration. a-kic is the competitive inhibitor to pyri doxal form of the enzyme and inhibitor con stant of a-kic was obtained to be 3.8 mm by Dixon's plot (Fig. 4). To calculate Km value for L-glutamate, the data of Fig. 4 was re plotted to double reciprocal plot. Obtained apparent Km values for L-glutamate were plotted against a-kic concentration (Fig. 5). From intersections to horizontal and vartical axes, inhibitor constant for a-kic and Km value for L-glutamate were estimated to be 3.8 mm and 3.2 mm, respectively. Km value for a-kic was calculated from the equation, S=_??_22) Here, S is the concentration of a-kic which gives apparent maximal velocity TABLE III. AMINO ACCEPTOR AND DONOR SPECIFICITY Pyru, pyruvate; a-kb, a-ketobutyrate; a-kiv, a-ketoisovalerate; L-Abu, L-a-aminobutyrate.
4 1174 Y. KOIDE, M. HONMA and T. SHIMOMURA FIG. 4. Dixon's Plot of L-Glutamate-a-KIC Tran samination. The reaction mixture of 0.4 ml contained 0.04 µmole of pyridoxal 5'-phosphate and various amounts of L-glutamate and a-kic in 0.1 M potassium phosphate buffer (ph 8.0). FIG. 6. Effect of ƒà-mercaptoethanol on Enzyme Activity. The enzyme was treated with each concentration of ƒà-mercaptoethanol for 10 min ( \ ) or 20 min ( œ \ œ) at 30 Ž, and preincubated with pyridoxal 5'-phosphate for 10 min, then incubated with sub strates for 10 min. captoethanol (Fig. 6). In subsequent ex periments, the activated enzyme was prepared by the treatment with 0.1 M ƒà-mercaptoethanol in 0.1 M potassium phosphate buffer (ph 8.0) for 20 min at 30 Ž. Michaelis constants of 0.1 M ƒà-mercapto ethanol-activated enzyme FIG. 5. Estimation of Km Value for L-Glutamate and Inhibitor Constant for a-kic. In the forward reaction at ph 8.0, Km The data of Fig. 4 was replotted to double reciprocal plot and obtained apparent Km values for L-glutamate were plotted against a-kic concentration to calculate Km value for L-glutamate and Ki value for a-kic. in Fig. 3. Km value for a-kic (Ka) was calculated to be 1.1 mm, when S=2.0 mm and Ki=3.8 mm were substituted in the equation. Effect of ƒà-mercaptoethanol on enzyme activity In general, branched chain amino acid aminotransferase and leucine aminotrans ferase are activated with ƒà-mercaptoetha nol.4 `6,8) Importance of SH groups in active center of the enzyme was pointed out because that a small amount of p-chloromercuribenzoate caused inactivation.8,12) This en zyme from Psendomonas sp. was similarly activated 2-fold with above 50 mm ƒà-mer FIG. 7. Double Reciprocal Plot of Initial Velocities against L-Leucine Concentration at Series of Fixed Concentrations of a-kg in Activated Enzyme. The experiments were carried out under the conditions described in Fig. 5. The used enzyme was activated with 0.1 M ƒà-mercaptoethanol.
5 Branched Chain Amino Acid Aminotransferase of Pseudomonas sp FIG. 8. Dixon's Plot of Isocaproic Acid Inhibition on L-Leucine-a-KG Transamination. The reaction mixture of 2.8 ml contained 0.28 ƒêmole of pyridoxal 5'-phosphate, 14 ƒêmoles of a-kg and various amounts of L-leucine and isocaproic acid in 0.1 M potassium phosphate buffer (ph 8.0). values were calculated to be 1.2 mm for L- leucine and 0.3 mm for a-kg (Fig. 7). In comparison with unactivated enzyme, ac tivated enzyme revealed greater Km value for L-leucine. This result suggests the participa tion of SH groups in the binding of L-leucine to enzyme. Inhibition of transamination by carboxylic acids It was reported that carboxylic acids as substrate analog are inhibitor of branched chain amino acid aminotransferase from pig heart. 9) Then, a series of mono- and di carboxylic acids were tested as inhibitor of transamination between L-leucine and a-kg. Both unactivated and activated enzymes were effectively inhibited by long chain mono carboxylic acids (Table IV). It is of interest that isocaproic acid which is substrate analog TABLE IV. INHIBITION BY CARBOXYLIC ACIDS The reaction mixture (2.8 ml) contained 5.6 µmoles of L-leucine and a-kg, and 56 ƒêmoles of carboxylic acid. of leucine is more effective inhibitor, but glutaric acid which is substrate analog of a-kg is less effective inhibitor. Inhibitor constants of isocaproic acid to pyridoxal form were measured as to unactivated and activated enzymes by the method of Velick and Vavra.21) It was found that isocaproic acid was a competitive inhibitor to L-leucine (Fig. 8), and the inhibitor constants were obtained to be 6 mm for unactivated enzyme and 14 mm for activated enzyme. DISCUSSION Branched chain amino acid aminotrans ferase was partially purified from Pseudomonas sp., and by using aminohexyl-agarose, another enzyme which catalyzes transamination be tween branched chain amino acids and a-keto analogs was completely separated as shown in Fig. 1. Partially purified branched chain amino acid aminotransferase showed extremely lower reactivity for L-isoleucine and higher reactivity for L-methionine. Generally, this enzyme represents about equal reactivity on L-leucine and L-isoleucine2 `7,10 `13) and low reactivity on L-methionine.6,7,11,12) At this point, the enzyme of Pseudomonas sp. was different from those of other origins. From the data of kinetics and substrate specificity, it could be considered that L-leucine-a-KG reaction pair is physiologically the most dominant.
6 1176 Y. KOIDE, M. HONMA and T. SHIMOMURA SCHEME I. Regulation of Branched Chain Amino Acid Pool by Aminotransferase System. Recently the authors purified L-tryptophana-KIC aminotransferase from the same or ganism that catalyzes transamination from only aliphatic or aromatic amino acids to a-keto analogs20) (Fig. 1). These two trans amination systems seem to maintain the branched chain amino acid pool in this or ganism as described in Scheme I. Similar transaminases have been reported in pea sprouts, valine-glutamate and valine-isoleucine aminotransferases. 23) Branched chain amino acid aminotrans ferase of Pseudomonas sp. was activated with Ĉ-mercaptoethanol, and this activated enzyme showed different kinetic properties from unactivated enzyme, such as increasing in Km value for L-leucine, Ki value for isocaproic acid and the maximum velocity. These kinetic properties were different from those of pig heart enzyme by Taylor and Jenkins.9) Pig heart enzyme was similarly activated with 0.1 M Ĉ-mercaptoethanol, however, this ac tivated enzyme showed decreasing Km value for L-leucine. To elucidate these differences, we considered the existence of S-S linkage in unactivated enzyme and SH groups in ac tivated enzyme from Pseudomonas sp. in the region of side-chain binding site for L- leucine. REFERENCES 1) Y. Koide, M. Honma and T. Shimomura, Agric. Biol. Chem., 41, 781 (1977). 2) A. Ichihara and E. Koyama, J. Biochem., 59,160 (1966). 3) A. Ichihara, H. Takahashi, K. Aki and A. Shirai, Biochem. Biophys. Res. Commun., 26, 674 (1967). 4) K. Aki, K. Ogawa, A. Shirai and A. Ichihara, J. Biochem., 62, 610 (1967). 5) K. Aki, A. Yokojima and A. Ichihara, ibid., 65, 539 (1969). 6) K. Ogawa, A. Yokojima and A. Ichihara, ibid., 68, 901 (1970). 7) R. T. Taylor and W. T. Jenkins, J. Biol. Chem., 241, 4396 (1966). 8) R. T. Taylor and W. T. Jenkins, ibid., 241, 4406 (1966). 9) R. T. Taylor and W. T. Jenkins, ibid., 245, 4880 (1970). 10) M. S. Coleman and F. B. Armstrong, Biochim. Biophys. Acta, 227, 56 (1971). 11) J. E. Norton and J. R. Sokatch, ibid., 206, 261 (1970). 12) M. Collins and R. P. Wagner, Arch. Biochem. Biophys., 155, 184 (1973). 13) D. Rudman and A. Meister, J. Biol. Chem., 200, 591 (1953). 14) R. Raunio, Acta Chem. Scand., 22,2733 (1968). 15) R. F. Itzhaki and D. M. Gill, Annal. Biochem., 9, 401 (1964). 16) R. T. Taylor and W. T. Jenkins, J. Biol. Chem., 241, 4391 (1966). 17) T. Tochikura, T. Tachiki, K. Nakahama, A.
7 Branched Chain Amino Acid Aminotransferase of Pseudomonas sp Baich and V. H. Cheldelin, Agric. Biol. Chem., 37, 1611 (1973). 18) J. G. Heathcote, Biochem. J., 97, 15 p (1965). 19) S. Shaltiel and Zui Er-EL, Proc. Natl. Acad. Sci. U.S.A., 70, 778 (1973). 20) Y. Koide, M. Honma and T. Shimomura, in pre paration. 21) S. F. Velick and J. Vavra, J. Biol. Chem., 237, 2109 (1962). 22) W. W. Cleland, "The Enzymes," 3rd Ed. Vol. II, ed. by P. D. Boyer, Academic Press Inc., New York, 1970, p ) Z. S. Kagan and A. S. Dronov, Dokl. Akad. Nauk. SSSR., 179, 1236 (1968).
Transaminase of Branched Chain Amino Acids
The Journal of Biochemistry, Vol. 59, No. 2, 1966 Transaminase of Branched Chain Amino Acids I. Branched Chain Amino Acids-a-Ketoglutarate Transaminase By AKIRA ICHIHARA* and Eizo KOYAMA (From the Department
More informationDAPA and desthiobiotin (DTB). The present paper deals with the mode of inhibition of
222 THE JOURNAL OF ANTIBIOTICS MAR. 1975 STUDIES ON THE MODE OF ACTION OF ICLENOMYCIN KUNIMOTO HOTTA, TAKER KITAHARA and YOSHIRO OKI Institute of Microbial Chemistry, Kamiosaki, Shinagawa-ku, Tokyo, Japan
More informationControl of Glycolaldehyde Dehydrogenase in Vitamin B6 Biosynthesis. in Escherichia coli B õ. Hiroshi MORITA, Yoshiki TANI and Koichi OGATA*
Agric. Biol. Chem., 42 (1), 69 `73, 1978 Control of Glycolaldehyde Dehydrogenase in Vitamin B6 Biosynthesis in Escherichia coli B õ Hiroshi MORITA, Yoshiki TANI and Koichi OGATA* Department of Agricultural
More informationEffects of Amino Acids and Glutathione on Rat Liver Histidase Activity in vitro
[Agr. Biol. Chem., Vol. 34, No. 5, p. 710-714, 1970] Effects of Amino Acids and Glutathione on Rat Liver Histidase Activity in vitro By Katuhiko NODA Department of Nutrition, School of Medicine, Tokushima
More informationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Vol. 62, No. 2, 19Z5 L-KYNURENINE AMINOTRANSFERASE AND L-~-AMINOADIPATE AMINOTRANSFERASE. I. EVIDENCE FOR IDENTITY Michael C. Tobes and Merle Mason Department of Biological Chemistry, The University of
More informationPrerequisites Protein purification techniques and protein analytical methods. Basic enzyme kinetics.
Case 19 Purification of Rat Kidney Sphingosine Kinase Focus concept The purification and kinetic analysis of an enzyme that produces a product important in cell survival is the focus of this study. Prerequisites
More informationTRANSAMINASES IN SMOOTH BRUCELLA ABORTUS, STRAIN 19
TRANSAMINASES IN SMOOTH BRUCELLA ABORTUS, STRAIN 19 BY ROBERT A. ALTENBERN AND RILEY D. HOUSEWRIGHT (From the Chemical Corps Biological Laboratories, Camp Detrick, Frederick, Maryland) (Received for publication,
More informationStudies on Kojic Acid Metabolism by Microorganisms
[Agr. Biol. Chem., Vol. 35, No. 13, p. 2025-2032, 1971] Studies on Kojic Acid Metabolism by Microorganisms Part XI. Comenic Aldehyde Dehydrogenaset õ (5-Methoxy Comenic Aldehyde Dehydrogenase) By Jun IMOSE,
More informationCase 19 Purification of Rat Kidney Sphingosine Kinase
Case 19 Purification of Rat Kidney Sphingosine Kinase Focus concept The purification and kinetic analysis of an enzyme that produces a product important in cell survival is the focus of this study. Prerequisites
More informationStudies on Barley and Malt Amylases. Part XIX. Activation of Zymogen Ĉ-amylase in vivo and Amylase. Formation in Isolated Aleurone Layers
[Agr. Biol. Chem., Vol. 36, No. 3, p. 378 `382, 1972] Studies on Barley and Malt Amylases Part XIX. Activation of Zymogen Ĉ-amylase in vivo and Amylase Formation in Isolated Aleurone Layers By Ryu SHINKE
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 informationA Component of Wheat Flour Globulin Polymerized at Alkaline Sides and Depolymerized by Reduction Reversibly
Agric. Biol. Chem., 42 (7), 1397 `1402, 1978 A Component of Wheat Flour Globulin Polymerized at Alkaline Sides and Depolymerized by Reduction Reversibly Masaki TERADA, Junichi MINAMI and Takehiko YAMAMOTO*'
More informationStudies on the Myrosinase in Mustard Seed. Part I. The Chromatographic Behaviors of the Myrosinase Some of its Characteristics*
[Agr. Biol. Chem., Vol. 31, No. 1, p. 1826, 1967] Studies on the Myrosinase in Mustard Seed Part I. The Chromatographic Behaviors of the Myrosinase and Some of its Characteristics* By Isao TsuRUO**, Mizuho
More informationMicrobial Production of L-Threonine. Part III. Production by Methionine and Lysine Auxotrophs. Derived from ƒ -Amino-ƒÀ-hydroxyvaleric Acid Resistant
I [Agr. Biol. Chem., Vol. 36, No. 7, p. 12091216, 1972] Microbial Production of L-Threonine Part III. Production by Methionine and Lysine Auxotrophs Derived from ƒ -Amino-ƒÀ-hydroxyvaleric Acid Resistant
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 informationMBB 694:407, 115:511. Please use BLOCK CAPITAL letters like this --- A, B, C, D, E. Not lowercase!
MBB 694:407, 115:511 First Test Severinov/Deis Tue. Sep. 30, 2003 Name Index number (not SSN) Row Letter Seat Number This exam consists of two parts. Part I is multiple choice. Each of these 25 questions
More informationspecificity of the formaldehyde dehydrogenase from Pseudomonasputida
Agric. Biol Chem., 48 (3), 597~601, 1984 597 Substrate Specificity of Dehydrogenase from Pseudomonasputida Susumu Ogushi, Makoto Ando* and Daisuke Tsuru Faculty of Pharmaceutical Sciences, Nagasaki University,
More informationON THE DIFFERENCE IN ADSORPTION ON SEPHADEX GEL OF THE DEXTRANSUCRASE OF STREPTOCOCCUS BOVIS GROWN ON SUCROSE AND GLUCOSE MEDIA
J. Gen. App!. Microbiol., 34, 213-219 (1988) ON THE DIFFERENCE IN ADSORPTION ON SEPHADEX GEL OF THE DEXTRANSUCRASE OF STREPTOCOCCUS BOVIS GROWN ON SUCROSE AND GLUCOSE MEDIA TOSHIRO HAYASHI, RYO IOROI,*
More informationGlutathione Synthesis in Human Erythrocytes
Glutathione Synthesis in Human Erythrocytes II. PURIFICATION AND PROPERTIES OF THE ENZYMES OF GLUTATHIONE BIOSYNTHESIS PHILI W. MAjEUS, M. J. BRAUNER, M. B. SMITH, and VIRGINIA MINNICH From the Departments
More informationPDF hosted at the Radboud Repository of the Radboud University Nijmegen
PDF hosted at the Radboud Repository of the Radboud University Nijmegen The following full text is a publisher's version. For additional information about this publication click this link. http://hdl.handle.net/2066/142604
More informationNOVEL SUBSTRATES OF YEAST ALCOHOL DEHYDROGENASE--4. ALLYL ALCOHOL AND ETHYLENE GLYCOL
pages 1-8 Received lune 15, 1998. Accepted July 6, 1998. NOVEL SUBSTRATES OF YEAST ALCOHOL DEHYDROGENASE--4. ALLYL ALCOHOL AND ETHYLENE GLYCOL Svetlana Trivid 1 and Vladimir Leskovac 2. I Faculty of Science
More informationGlUCOSE METABOlISM AND AMINO ACID IN. By YASUZO TSUKADA, YUTAKA NAGATA, SHUSUKE HIRANO AND GENKICHIRO TAKAGAKI
The Journal of Biochemistry, Vol. 45, No. 12, 1958 GlUCOSE METABOlISM AND AMINO ACID IN BRAIN SlICES By YASUZO TSUKADA, YUTAKA NAGATA, SHUSUKE HIRANO AND GENKICHIRO TAKAGAKI (From the Department of Physioloey,
More informationAcetyl CoA Carboxylase: The Purified Transcarboxylase Component
Proc. Nat. Acad. Sci. USA Vol. 68, No. 6, pp. 12591263, June 1971 Acetyl CoA Carboxylase: The Purified Transcarboxylase Component (acyl CoA binding/carboxylation/exchange reactions/biotin) ALFRED W. ALBERTS,
More informationThe Effects of N-thiophosphoryl Amino Acids on the Activity of Green Crab (Scylla Serrata) Alkaline Phosphatase
Vol. 45, No. 3, July 1998 Pages 465-473 The Effects of N-thiophosphoryl Amino Acids on the Activity of Green Crab (Scylla Serrata) Alkaline Phosphatase Qing-Xi Chen 1'3, Hai-Yan Lu 2, Chun-Ming Zhu 1,
More informationNonidentity of the Aspartate and the Aromatic Aminotransferase Components of Transaminase A in Escherichia colil
JOURNAL OF BACrERIOLOGY, OCt. 1972, p. 365-371 Copyright i 1972 American Society for Microbiology Vol. 112, No. 1 Printed in U.S.A. Nonidentity of the Aspartate and the Aromatic Aminotransferase Components
More informationBiochemical Studies on the Mineral Components in Sake Yeast. Part V. The Relationship of the Mineral Composition of Yeast to Fermentation
[Agr, Biol. Chem. Vol. 30, No. 9, p. 925 `930, 1966] Biochemical Studies on the Mineral Components in Sake Yeast Part V. The Relationship of the Mineral Composition of Yeast to Fermentation By Tsuyoshi
More informationThe Conservation of Homochirality and Prebiotic Synthesis of Amino Acids
The Conservation of Homochirality and Prebiotic Synthesis of Amino Acids Harold J. Morowitz SFI WORKING PAPER: 2001-03-017 SFI Working Papers contain accounts of scientific work of the author(s) and do
More informationBiosynthesis of Vitamin B6
THE JOURNAL OF VITAMINOLOGY 16, 154-159 (1970) Biosynthesis of Vitamin B6 I. Incorporation of 14C-Glycerol, Aspartic Acid and Leucine into Vitamin B6 RYOKUERO SUZUE1 AND YUKIo HARUNA2,3 Department of Medical
More informationBACTERIAL FORMATION OF L GLUTAMIC ACID FROM ACETIC ACID IN THE GROWING
J. Gen. Vol. Appl. 7, No. Microbiol. 1, 1961 BACTERIAL FORMATION OF L GLUTAMIC ACID FROM ACETIC ACID IN THE GROWING CULTURE MEDIUM'' (II) GROWTH AND L GLUTAMATE ACCUMULATION IN A CHEMICALLY DEFINED MEDIUM
More informationIdentification of Three Major Components in Fish Sarcoplasmic Proteins
Nippon Suisan Gakkaishi 54(6), 999-1004 (1988) Identification of Three Major Components in Fish Sarcoplasmic Proteins Takayuki Nakagawa,*1 Shugo Watabe,*2 and Kanehisa Hashimoto*2 (Received November 6,
More informationPrerequisites Amino acid synthesis and degradation pathways. Integration of amino acid metabolic pathways with carbohydrate metabolic pathways.
Case 30 Phenylketonuria Focus concept The characteristics of phenylalanine hydroxylase, the enzyme missing in persons afflicted with the genetic disorder phenylketonuria (PKU), are examined. Prerequisites
More informationUDP-Glucose Pyrophosphorylase from Potato Tuber: Purification and Characterization1
J. Biochem. 106, 528-532 (1989) UDP-Glucose Pyrophosphorylase from Potato Tuber: Purification and Characterization1 Kenichi Nakano,2 Yasuko Omura,3 Mitsao Tagaya, and Toshio Fukui4 The Institute of Scientific
More informationStudent Number: THE UNIVERSITY OF MANITOBA April 10, 2006, 1:30 AM - 4:30 PM Page 1 (of 4) Biochemistry II Laboratory Section Final Examination
Name: Student Number: April 10, 2006, 1:30 AM - 4:30 PM Page 1 (of 4) Biochemistry II Laboratory Section Final Examination Examiner: Dr. A. Scoot 1. Answer ALL questions in the space provided. 2. The back
More informationSUMMARY AND CONCLUSION
SUMMARY AND CONCLUSION A potential lipase producing marine fungus was selected among 14 lipase producers isolated from seawater and sediments of South Indian coastal environments which was identified as
More informationSTUDIES ON ASPIRIN ESTERASE OF HUMAN SERUM. Masako MORIKAWA, Michiko INOUE, Minoru TSUBOI. and Mamoru SUGIURA*
STUDIES ON ASPIRIN ESTERASE OF HUMAN SERUM Masako MORIKAWA, Michiko INOUE, Minoru TSUBOI and Mamoru SUGIURA* Department of Pharmacology, Tokyo College of Pharmacy, Horinouchi, Hachioji-shi, Tokyo 192-03,
More informationMidterm 1 Last, First
Midterm 1 BIS 105 Prof. T. Murphy April 23, 2014 There should be 6 pages in this exam. Exam instructions (1) Please write your name on the top of every page of the exam (2) Show all work for full credit
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 informationBiodegradative Threonine Dehydratase. Reduction of Ferricyanide by an Intermediate of the Enzyme-Catalyzed Reaction
Eur. J. Biochem. Y I, 527-532 (1978) Biodegradative Threonine Dehydratase. Reduction of Ferricyanide by an Intermediate of the Enzyme-Catalyzed Reaction Prasanta DATTA and Ranjan BHADRA Department of Biological
More informationEFFECT OF SOME AMINO ACIDS ON THE GROWTH AND L-GLUTAMIC ACID FERMENTATION BY AN AUXOTROPHIC MUTANT Micrococcus glutamicus AB 100.
S. Ganguly et. al. / International Journal on Pharmaceutical and Biomedical Research (IJPBR) Vol. 2(1), 2011, 21-25 EFFECT OF SOME AMINO ACIDS ON THE GROWTH AND L-GLUTAMIC ACID FERMENTATION BY AN AUXOTROPHIC
More informationSerrata) Alkaline Phosphatase
Vol. 41, No. 5, April 1997 BIOCHEMISTRY and MOLECULAR BIOLOGY INTERNATIONAL Pages 951-959 An Essential Tryptophan Residue of Green Crab (Syclla Serrata) Alkaline Phosphatase Wen-Zhu Zheng 1, Qing-Xi Chen
More informationIntroduction to Biochemistry Midterm exam )ومن أحياها(
Introduction to Biochemistry Midterm exam 2016-2017 )ومن أحياها( 1. Which of the following amino (in a peptide chain) would probably be found at a beta bend or turn? a. lysine * b. Gly c. arg d. asn 2.
More informationBiochemistry: A Short Course
Tymoczko Berg Stryer Biochemistry: A Short Course Second Edition CHAPTER 30 Amino Acid Degradation and the Urea Cycle 2013 W. H. Freeman and Company Chapter 30 Outline Amino acids are obtained from the
More informationSynthesis and Degradation of Liver Acetyl Coenzyme A Carboxylase
Proc. Nat. Acad. Sci. USA Vol. 68, No. 9, pp. 2288-2292, September 1971 Synthesis and Degradation of Liver Acetyl Coenzyme A Carboxylase in Genetically Obese Mice (increased hepatic lipogenesis/immunochemical
More informationReconstitution of Neutral Amino Acid Transport From Partially Purified Membrane Components From Ehrlich Ascites Tumor Cells
Journal of Supramolecular Structure 7:481-487 (1977) Molecular Aspects of Membrane Transport 5 1 1-5 17 Reconstitution of Neutral Amino Acid Transport From Partially Purified Membrane Components From Ehrlich
More informationSolubilization and Activation of Membrane-bound Acid Protease of Aspergillus oryzae
Agric. Biol. Chem., 41 (11), 2125 `2130, 1977 Solubilization and Activation of Membrane-bound Acid Protease of Aspergillus oryzae Yoshio TSUJITA and Akira ENDO Fermentation Research Laboratories Sankyo
More informationOF TRANSAMINASE IN RAT TISUES
OF TRANSAMINASE IN RAT TISUES KOZO YAMADA, SHUNJI SAWAKI, AKIRA FUKUMURA AND MASARU HAYASHID epartment of Internal Mcdicine, Faculty of Medicine, Nagoya University, agoya Showa-ku, N (Received July 30,
More informationLecture 10 - Protein Turnover and Amino Acid Catabolism
Lecture 10 - Protein Turnover and Amino Acid Catabolism Chem 454: Regulatory Mechanisms in Biochemistry University of Wisconsin-Eau Claire 1 Introduction 2 Proteins are degraded into amino acids. Protein
More informationNitrogen Metabolism. Overview
Nitrogen Metabolism Pratt and Cornely Chapter 18 Overview Nitrogen assimilation Amino acid biosynthesis Nonessential aa Essential aa Nucleotide biosynthesis Amino Acid Catabolism Urea Cycle Juicy Steak
More informationIdentification of NADPH-thioredoxin reductase system
Proc. Nat. Acad. Sci. USA Vol. 72, No. 11, pp. 4233-4237, November 1975 Biochemistry Identification of NADPH-thioredoxin reductase system in Euglena gracilis* (ribonucleotide reduction) S. MUNAVALLIO,
More informationSTUDIES ON LIPASE I. ON THE ACTIVATION OF PANCREAS LIPASE. (From the Department of Medicical Chemistry, Faculty of Medicine, Kyoto University, Kyoto)
The Journal of Biochemistry, Vol. 38, No. 2. STUDIES ON LIPASE I. ON THE ACTIVATION OF PANCREAS LIPASE BY TOSHIICHI YAMAMOTO (From the Department of Medicical Chemistry, Faculty of Medicine, Kyoto University,
More informationCysteine and Growth Inhibition of Escherichia coli:
JOURNAL OF BACTERIOLOGY, Feb. 1981, p. 1031-1035 0021-9193/81/021031-05$02.00/0 Vol. 145, No. 2 Cysteine and Growth Inhibition of Escherichia coli: Threonine Deaminase as the Target Enzyme CHARLES L. HARRIS
More informationpreparation which is available contains an oligo-1,4-0 1,4-glucantransferase
THE PROPERTIES OF AN OLIGO-1,4 -- 1,4-GLUCANTRANSFERASE FROM ANIMAL. TISSUES* BY DAVID H. BROWN AND BARBARA ILLINGWORTH DEPARTMENT OF BIOLOGICAL CHEMISTRY, WASHINGTON UNIVERSITY SCHOOL OF MEDICINE, SAINT
More informationTRANSPORT OF AMINO ACIDS IN INTACT 3T3 AND SV3T3 CELLS. Binding Activity for Leucine in Membrane Preparations of Ehrlich Ascites Tumor Cells
Journal of Supramolecular Structure 4:441 (401)-447 (407) (1976) TRANSPORT OF AMINO ACIDS IN INTACT 3T3 AND SV3T3 CELLS. Binding Activity for Leucine in Membrane Preparations of Ehrlich Ascites Tumor Cells
More informationStudent Number: To form the polar phase when adsorption chromatography was used.
Name: Student Number: April 14, 2001, 1:30 AM - 4:30 PM Page 1 (of 4) Biochemistry II Lab Section Final Examination Examiner: Dr. A. Scoot 1. Answer ALL questions in the space provided.. 2. The last page
More informationAmino acid metabolism
Amino acid metabolism The important reaction commonly employed in the breakdown of an amino acid is always the removal of its -amino group. The product ammonia is excreted after conversion to urea or other
More informationINTESTINAL ABSORPTION OF AMINO ACIDS I. THE EFFECT OF VITAMIN B6 ON THE ABSORPTION OF L-AMINO ACIDS THROUGH THE INTESTINE
The Journal of Biochemistry, Vol. 47, No. 1, 1960 INTESTINAL ABSORPTION OF AMINO ACIDS I. THE EFFECT OF VITAMIN B6 ON THE ABSORPTION OF L-AMINO ACIDS THROUGH THE INTESTINE By HITOSHI AKEDO, TADASHI SUGAWA,
More information0010 Amino Acids 40 Profile - Plasma
Accession #: Order #: G1234567 Date Collected: Date Received: 01/22/2013 Reference #: Patient: Date of Birth: 02/05/1962 Date of Report: Telephone: 7704464583 Ordering Physician: 1234 Main St. Anywhere,
More informationEFFECT OF SULFUR-CONTAINING AMINO ACIDS ON THE PRODUCTION OF THIAMINE BY ESCHERICHIA COLI1
THE JOURNAL OF VITAMINOLOGY 9, 183-187 (1963) EFFECT OF SULFUR-CONTAINING AMINO ACIDS ON THE PRODUCTION OF THIAMINE BY ESCHERICHIA COLI1 MASUO AKAGI AND HIROSHI KUMAOKA2 Faculty of Pharmaceutical Science,
More informationA NEW COFACTOR REQUIRED FOR THE ENZYMATIC CONVERSION OF PHENYLALANINE TO TYROSINE*
A NEW COFACTOR REQUIRED FOR THE ENZYMATIC CONVERSION OF PHENYLALANINE TO TYROSINE* BY SEYMOUR KAUFMAN (From the Laboratory of Cellular Pharmacology, National Institute of Mental Health, United States Department
More informationM1 - Renal, Fall 2007
University of Michigan Deep Blue deepblue.lib.umich.edu 2007-09 M1 - Renal, Fall 2007 Lyons, R.; Burney, R. Lyons, R., Burney, R. (2008, August 07). Renal. Retrieved from Open.Michigan - Educational Resources
More informationFate of Dietary Protein
Fate of Dietary Protein Dietary protein Stomach: l, pepsin Denatured and partially hydrolyzed protein (large polypeptides) small intestine: proteases Amino acids and dipeptides intestinal lining: proteases
More informationJ. Physiol. (I956) I33,
626 J. Physiol. (I956) I33, 626-630 ACTIVE TRANSPORT OF AMINO ACIDS BY SACS OF EVERTED SMALL INTESTINE OF THE GOLDEN HAMSTER (MESOCRICETUS AURATUS) BY G. WISEMAN From the Department of Physiology, University
More informationAmino Acid Metabolism
Amino Acid Metabolism Fate of Dietary Protein Dietary protein Stomach: l, pepsin Denatured and partially hydrolyzed protein (large polypeptides) small intestine: proteases Amino acids and dipeptides intestinal
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 informationMetabolism of proteins and amino acids
BIOQUÍMICA E BIOLOGIA CELULAR António Ascensão, José Magalhães Metabolism of proteins and amino acids Faculdade de Desporto, Universidade do Porto, 1º Ciclo, 1º Ano 202_2013 Humans degradation of ingested
More informationHydrophobic Interaction Chromatography
1 Hydrophobic Interaction Chromatography Philip Cummins 1 and Brendan O Connor 1,2 1 School of Biotechnology, 2 Irish Separation Science Cluster, Dublin City University, Dublin 9, Republic of Ireland.
More informationThe diagram below summarizes the conversion of the twenty standard amino acids. Copyright Mark Brandt, Ph.D. 23
Amino acid breakdown Amino acids comprise one of the three major energy sources for animals. They are an especially important energy source for carnivorous animals, and for all animals during early starvation
More informationStudies on the Induced Synthesis of Maleate cistrans Isomerase by Malonate
Agricultural and Biological Chemistry ISSN: 2-1369 (Print) (Online) Journal homepage: https://www.tandfonline.com/loi/tbbb19 Studies on the Induced Synthesis of Maleate cistrans Isomerase by Malonate Yoshichika
More informationSubstrate Specificity and Salt Inhibition of Five Proteinases Isolated from the Pyloric Caeca and Stomach of Sardine
Agric. Biol. Chem., 46 (6), 1565~1569, 1982 1565 Substrate Specificity and Salt Inhibition of Five Proteinases Isolated from the Pyloric Caeca and Stomach of Sardine Minoru Noda, Thanh Vo Van, Isao Kusakabe
More informationbiotin per 409,000 gm of protein.4 Ryder et al.4 have reported preliminary investigations
ACETYL COA CARBOXYLASE, I. REQUIREMENT FOR TWO PROTEIN FRACTIONS* BY ALFRED W. ALBERTS AND P. R. VAGELOS DEPARTMENT OF BIOLOGICAL CHEMISTRY, WASHINGTON UNIVERSITY SCHOOL OF MEDICINE, ST. LOUIS, MISSOURI
More informationاالمتحان النهائي لعام 1122
االمتحان النهائي لعام 1122 Amino Acids : 1- which of the following amino acid is unlikely to be found in an alpha-helix due to its cyclic structure : -phenylalanine -tryptophan -proline -lysine 2- : assuming
More informationSulfate Reduction in Escherichia coli. (From the Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Tohyo)
The Journal of Biochemistry, Vol. 50, No. 6, 1961 Sulfate Reduction in Escherichia coli By DAISABURO FUJIMOTO* and MAKOTO ISHIMOTO (From the Department of Biophysics and Biochemistry, Faculty of Science,
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 informationMetabolic Classification of the Amino Acids
Metabolic Classification of the Amino Acids *Essential and Non-essential * Glucogenic and Ketogenic 1 Essential Amino Acids Of the 20 amino acids that make up proteins 10 of them can be synthesized by
More information0010 Amino Acid Analysis - 40 Plasma
770.446.5483 770.441.2237 This report contains reference range adjustments from routine revalidation procedures. It also contains the following three upgrades: 1) The amino acids have been reorganized
More informationAkiyoshi HOSONO and Fumisaburo. (Faculty of Agriculture, Shinshu University, Ina, Nagano-Ken, Japan) (Received for Publication on May, 7, 1970)
The lipolytic properties of Candida mycoderma and Debaryomyces kloeckeri isolated from limburger cheese and some properties of the lipases produced by these yeasts Akiyoshi HOSONO and Fumisaburo TOKITA
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 informationBiochemistry - I. Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture 1 Amino Acids I
Biochemistry - I Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture 1 Amino Acids I Hello, welcome to the course Biochemistry 1 conducted by me Dr. S Dasgupta,
More informationTHE UNIVERSITY OF MANITOBA. DATE: Oct. 22, 2002 Midterm EXAMINATION. PAPER NO.: PAGE NO.: 1of 6 DEPARTMENT & COURSE NO.: 2.277/60.
PAPER NO.: PAGE NO.: 1of 6 GENERAL INSTRUCTIONS You must mark the answer sheet with pencil (not pen). Put your name and enter your student number on the answer sheet. The examination consists of multiple
More informationINHIBITION OF PHENYLALANINE HYDROXYLASE, A PTERIN-REQUIRING MONOOXYGENASE, BY AND ITS DERIVATIVES
458 THE JOURNAL OF ANTIBIOTICS APR. 1982 INHIBITION OF PHENYLALANINE HYDROXYLASE, A PTERIN-REQUIRING MONOOXYGENASE, BY OUDENONE AND ITS DERIVATIVES SHINICHI KOIZUMI, TOSHIHARU NAGATSU, HIRONOBU IINUMA*,
More informationبسم هللا الرحمن الرحيم
بسم هللا الرحمن الرحيم Q1: the overall folding of a single protein subunit is called : -tertiary structure -primary structure -secondary structure -quaternary structure -all of the above Q2 : disulfide
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 informationI mutants accumulate pyruvate when growing in the presence of isoleucine and
THE iv-3 MUTANTS OF NEUROSPORA CRASSA 11. ACTIVITY OF ACETOHYDROXY ACID SYNTHETASE DINA F. CAROLINE, ROY W. HARDINGZ, HOMARE KUWANA3, T. SATYANARAYANA AND R.P. WAGNER4 Genetics Foundation, The University
More informationJ. Nutr. Sci. Vitaminol., 38, , Note. in Tissues
J. Nutr. Sci. Vitaminol., 38, 517-521, 1992 Note A Simple Enzymatic Quantitative in Tissues Analysis of Triglycerides Hiroshi DANNO, Yuu JINCHO, Slamet BUDIYANTO, Yuji FURUKAWA, and Shuichi KIMURA Laboratory
More informationNitrogen Metabolism. Pratt and Cornely Chapter 18
Nitrogen Metabolism Pratt and Cornely Chapter 18 Overview Nitrogen assimilation Amino acid biosynthesis Nonessential aa Essential aa Nucleotide biosynthesis Amino Acid Catabolism Urea Cycle Juicy Steak
More informationAMINO ACIDS STRUCTURE, CLASSIFICATION, PROPERTIES. PRIMARY STRUCTURE OF PROTEINS
AMINO ACIDS STRUCTURE, CLASSIFICATION, PROPERTIES. PRIMARY STRUCTURE OF PROTEINS Elena Rivneac PhD, Associate Professor Department of Biochemistry and Clinical Biochemistry State University of Medicine
More informationR.'ecent evidence strongly suggests that
Activators and inhibitors of lens aldose reductase /. A. Jedziniak and J. H. Kinoshita Aldose reductase in a highly purified state is unstable. It requires the presence of thiol groups to maintain it in
More informationThe Effect of Carboxylates and Halides on L-Lysine 6-Aminotransferase-Catalyzed Reactions
/. Biochem. 95, 559-565 (1984) The Effect of Carboxylates and Halides on L-Lysine 6-Aminotransferase-Catalyzed Reactions Tohru YOSHIMURA, Katsuyuki TANIZAWA, Hidehiko TANAKA, and Kenji SODA Laboratory
More information10 mm KCl in a Ti-15 zonal rotor at 35,000 rpm for 16 hr at
Proc. Nat. Acad. SCi. USA Vol. 68, No. 11, pp. 2752-2756, November 1971 Translation of Exogenous Messenger RNA for Hemoglobin on Reticulocyte and Liver Ribosomes (initiation factors/9s RNA/liver factors/reticulocyte
More informationAmino Acid Oxidation and the Urea Cycle
Amino Acid Oxidation and the Urea Cycle Amino Acids: Final class of biomolecules whose oxidation contributes significantly to the generation of energy Undergo oxidation in three metabolic circumstances
More informationASPARTATE METABOLISM AND ASPARAGINE SYNTHESIS IN PLANT SYSTEMS*
ASPARTATE METABOLISM AND ASPARAGINE SYNTHESIS IN PLANT SYSTEMS* BY GEORGE C. WEBSTER AND J. E. VARNERt (From the Kerckhoff Laboratories of Biology, California Institute of Technology, Pasadena, California)
More informationNITROGEN METABOLISM An Overview
1 University of Papua New Guinea School of Medicine and Health Sciences Division of Basic Medical Sciences Discipline of Biochemistry and Molecular Biology PBL Seminar & Health Sciences NITROGEN METABOLISM
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 informationBiochemistry: A Short Course
Tymoczko Berg Stryer Biochemistry: A Short Course Second Edition CHAPTER 30 Amino Acid Degradation and the Urea Cycle 2013 W. H. Freeman and Company In the cytosol of a cell amino groups from amino acids
More informationNitrogen Metabolism. Overview
Nitrogen Metabolism Pratt and Cornely Chapter 18 Overview Nitrogen assimilation Amino acid biosynthesis Nonessential aa Essential aa Nucleotide biosynthesis Amino Acid Catabolism Urea Cycle Juicy Steak
More informationSix Types of Enzyme Catalysts
Six Types of Enzyme Catalysts Although a huge number of reactions occur in living systems, these reactions fall into only half a dozen types. The reactions are: 1. Oxidation and reduction. Enzymes that
More informationWHY? 26/2/2010. Shimomura Y, Harris RA. J Nutr. 2006;136(1 suppl):232s-233s. BCAA buffer excessive amounts of Glutamate by converting it to Glutamine.
Branched Chain Amino Acids as Adjunctive Therapy to Ketogenic Diet Athanasios Evangeliou MD 4th Department of Pediatrics of the Aristotle University of Thessaloniki Papageorgiou Hospital Thessaloniki E-mail:
More informationCommon Enzymes of Branched-Chain Amino Acid Catabolism in Pseudomonas putida
JOURNAL OF BACTERIOLOGY, JUlY 1973, p. 198-204 Copyright i 1973 American Society for Microbiology Vol. 115, No. 1 Printed in U.S.A. Common Enzymes of Branched-Chain Amino Acid Catabolism in Pseudomonas
More informationEFFECT OF AN EXCESS INTAKE OF LEUCINE, WITH AND WITHOUT ADDITIONS OF VITAMIN B6 AND/OR NIACIN, ON TRYPTOPHAN AND NIACIN METABOLISM IN RATS
J. Nutr. Sci. Vitaminol., 23, 535-548, 1977 EFFECT OF AN EXCESS INTAKE OF LEUCINE, WITH AND WITHOUT ADDITIONS OF VITAMIN B6 AND/OR NIACIN, ON TRYPTOPHAN AND NIACIN METABOLISM IN RATS Itsiro NAKAGAWA and
More informationADSORPTION AND DESORPTION OF METAL IONS BY SYSTEMS BASED ON CELLULOSE DERIVATIVES THAT CONTAIN AMINO ACID RESIDUES"
(41) Vol. 41, No.6 (1985) T-235 (Received May 24, 1984) ADSORPTION AND DESORPTION OF METAL IONS BY SYSTEMS BASED ON CELLULOSE DERIVATIVES THAT CONTAIN AMINO ACID RESIDUES" By Toshihiko Sato, Shigenori
More information