The following corrections have been made in various reprints of the Lehninger Principles of Biochemistry, 3e. Turn to page ii of your text to determine which printing you have. For example, if your book has: Printing: 5 4 3, that indicates a printing, and you will want to note errors corrected in the and 5th printings. Page Location Correction Correction made in this printing 7 Third paragraph 96 First sentence of section The definitions of closed and isolated systems are reversed. Please correct to read, If the system exchanges neither matter nor energy with its surroundings, it is said to be isolated. If the system exchanges energy but not matter with its surroundings, it is a closed system; Change only about one of every 10 7 molecules to only about two in every 10 9 molecules. 118 Table 5-1 Proline should be in the Nonpolar, aliphatic R groups section instead of the Polar, uncharged R groups section. 119 Fig. 5-5 Proline should be in the Nonpolar, aliphatic R groups section instead of the Polar, uncharged R groups section. 119 End of the Insert Proline s aliphatic side chain has a distinctive cyclic first structure. The secondary amino (imino) group of Pro residues is paragraph held in a rigid conformation that reduces the structural flexibility of polypeptide regions containing proline. 120 Second paragraph Delete proline from the list of amino acids in this group. Delete the last two sentences of the paragraph. 5th
164 Fig. 6-4a,b The correct figures are: 165 Line 10 of Change Leu to Cys. section 167 Fig. 6-7 All images should be rotated 180 in the plane of the paper. 168 Fig. 6-8 The correct image is:
205 Fig. 7-2 The structure of the His residue bound to the heme group should be corrected. The correct image is: 215 Eqn 7-16 Should include: 215 Sentence preceding Eqn 7-17 Change P 50 to: 215 Eqn 7-17 Insert n before log P 50. 262 Table 8-6 The K m for catalase should be 1100 mm. 263 Table 8-7 Change acetylcholinesterase k cat from 140,000 to 14,000 313 Fig. 9-25b The three final hexagons that are dark blue (glucose) in the last molecule should be light blue (Neu5Ac). 353 Fig. 10-37 The colored bands visible in the capillary gel should be inverted. In other words, the yellow bands should be near the top of the gel and the blue bands near the bottom of the gel. 353 Fig. 10-37 In printings only, the bands in the capillary gel are in the 5th correct order, but there is a black band near the middle that should be yellow. 367 Box 11-1 Paragraph 1, change 18,000 kg to 3,600 kg 441 Last line Change to read: causes a cation to pass spontaneously inward 5th through [changes and insertions underlined] 442 Line 2 and Eqn 13-1 Change (C 2 /C 1 ) to (C in /C out ) 5th
442 Mid-page Delete the Nernst equation and the line above it. Sentence ends zero. 5th 464 Lines 9-10 Change sentence to read: The camp-gated Na + and Ca 2+ channels of the ciliary membrane open, and the influx of Na + and Ca 2+ produces [insertions underlined] 481 Problem 5 Line 4 should read on the ocean bottom, where the temperature is 60 C. [insertion underlined] In the table, the values for intracellular and extracellular concentrations are reversed. 488 Fig. 5 In caption, change alkaline to alkane 510 7 lines from The left side of the reversible reaction catalyzed by creatine kinase the bottom should read ADP + PCr (not ATP + PCr). 560 Box 15-4, The two semicircular reaction arrows showing interconversion of Fig. 1 NADP + and NADPH + H + should be reversed. 571 Fig. 16-6 At step 2, transpose acetyl group and hydrogen on the sulfur atoms 589 Fig. 16-16 Structure of glyoxylate should have a carboxylate and a carbonyl group, not two carboxylates.
590 Fig. 16 18 The cycle shown in the glyoxysome shows oxaloacetate in the wrong place. The corrected figure is:
633 Fig. 18-8 The wrong overlay was used on this figure. The figure should look like: 662 Fig. 19 2 The semiquinone radical should have an aromatic ring. 683 Eqn 19-11 The equation should read: 709 5 lines from Replace G = RT ph the bottom with G = 2.3RT ph 759 Fig. 20-37 In line 3 of the caption, delete (FBPase-2).
761 Fig. 20-39 In the mitochondrion, delete the O 2 that enters at the lower right Likewise, the last sentence of the caption should read Oxygen is consumed at two steps during photorespiration (shaded blue). 811 Fig. 21-42 In figure title and caption, change HMG-CoA synthase to HMG-CoA reductase. 819 Fig. 22-1 In the screened box at the bottom, change Nitrate to Nitrite 841 Fig. 22-23 At step 6, change 4CO 2 to 2CO 2. In the caption at step 3, change the enzyme name from uroporphyrinogen synthase to hydroxymethylbilane synthase. 841 Box 22-1 Line 7, change porphobilinogen deaminase to hydroxymethylbilane synthase. 876 Fig. 23-9 caption In lines 6-7, change 13 C-enriched glucose (not a radioisotope, and therefore not a health hazard) to A positron-emitting glucose analog (2-[ 18 F]-fluoro-2-deoxy-D-glucose). 938 Fig. 25-6a,b Extra double bond above N in guanine residues should be deleted. 973 Fig. 25-42 Adjust J gene subscripts. 1002 2 lines from bottom Change a different N atom to C-5 1047 Fig. 27-25 In the ribosome cartoon at the bottom of the figure, the trna bound in the A site should have AA 2 attached, not fmet.
1097 Fig. 28-26 and caption Figure should show (p)ppgpp instead of ppgpp. Caption should read (beginning with line 5) of pppgpp. A phosphohydrolase then cleaves off one phosphate to give ppgpp. The signal 1097 Line 10 In the equation, change ppgpp to (p)ppgpp. Index Entries for Chapter 15 (pp. 525-566) were off by one page (525 should be 526, etc.) in the first three printings.