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.
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 3rd printing, and you will want to note errors corrected in the 4th and 5th printings. Page
Location
7
Third paragraph
96
118
First sentence of section Table 5-1
119
Fig. 5-5
119
End of the first paragraph
120
Second paragraph
Correction
Correction made in this printing The definitions of closed and isolated systems are reversed. Please 5th 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; …” 4th Change “only about one of every 107 molecules” to “only about 9 two in every 10 molecules.” Proline should be in the “Nonpolar, aliphatic R groups” section instead of the “Polar, uncharged R groups” section. Proline should be in the “Nonpolar, aliphatic R groups” section instead of the “Polar, uncharged R groups” section. Insert “Proline’s aliphatic side chain has a distinctive cyclic structure. The secondary amino (imino) group of Pro residues is held in a rigid conformation that reduces the structural flexibility of polypeptide regions containing proline.” Delete “proline” from the list of amino acids in this group. Delete the last two sentences of the paragraph.
4th 4th 4th
4th
164
Fig. 6-4a,b
The correct figures are:
4th
165
Line 10 of section Fig. 6-7 Fig. 6-8
Change “Leu” to “Cys.”
4th
All images should be rotated 180° in the plane of the paper. The correct image is:
4th 4th
167 168
205
Fig. 7-2
The structure of the His residue bound to the heme group should be corrected. The correct image is:
4th
215
Eqn 7-16
Should include:
4th
215
Sentence preceding Eqn 7-17
Change “P50” to:
4th
215 262 263 313
Eqn 7-17 Table 8-6 Table 8-7 Fig. 9-25b
4th 4th 3rd 4th
353
Fig. 10-37
353
Fig. 10-37
367 441
Box 11-1 Last line
442
Line 2 and Eqn 13-1
Insert “n” before “log P50.” The Km for catalase should be 1100 mM. Change acetylcholinesterase kcat from 140,000 to 14,000 The three final hexagons that are dark blue (glucose) in the last molecule should be light blue (Neu5Ac). 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. In 4th printings only, the bands in the capillary gel are in the correct order, but there is a black band near the middle that should be yellow. Paragraph 1, change “18,000 kg” to “3,600 kg” Change to read: “…causes a cation to pass spontaneously inward through…” [changes and insertions underlined] Change “(C2/C1)” to “(Cin/Cout)”
4th
5th
3rd 5th 5th
442
Mid-page
Delete the Nernst equation and the line above it. Sentence ends “…zero.”
5th
464
Lines 9-10
3rd
481
Problem 5
488 510
571
Fig. 5 7 lines from the bottom Box 15-4, Fig. 1 Fig. 16-6
Change sentence to read: “The cAMP-gated Na+ and Ca2+ channels of the ciliary membrane open, and the influx of Na+ and Ca2+ produces…” [insertions underlined] 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. In caption, change “alkaline” to “alkane” The left side of the reversible reaction catalyzed by creatine kinase should read ADP + PCr (not ATP + PCr). The two semicircular reaction arrows showing interconversion of NADP+ and NADPH + H+ should be reversed. 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.
3rd
560
3rd
3rd 4th 4th 3rd
590
Fig. 16–18
The cycle shown in the glyoxysome shows oxaloacetate in the wrong place. The corrected figure is:
4th
633
Fig. 18-8
The wrong overlay was used on this figure. The figure should look like:
3rd
662 683
Fig. 19–2 Eqn 19-11
The semiquinone radical should have an aromatic ring. The equation should read:
4th 3rd
709
5 lines from the bottom Fig. 20-37
Replace ∆G = RT ∆pH with ∆G = 2.3RT ∆pH In line 3 of the caption, delete “(FBPase-2).”
4th
759
3rd
761
Fig. 20-39
811
Fig. 21-42
819
Fig. 22-1
841
Fig. 22-23
841
Box 22-1
876
Fig. 23-9 caption
938 973
Fig. 25-6a,b Fig. 25-42
1002
2 lines from bottom Fig. 27-25
1047
In the mitochondrion, delete the O2 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).” In figure title and caption, change “HMG-CoA synthase” to “HMG-CoA reductase.” In the screened box at the bottom, change “Nitrate” to “Nitrite”
4th
At step 6, change 4CO2 to 2CO2. In the caption at step 3, change the enzyme name from “uroporphyrinogen synthase” to “hydroxymethylbilane synthase.” Line 7, change “porphobilinogen deaminase” to “hydroxymethylbilane synthase.” In lines 6-7, change “13C-enriched glucose (not a radioisotope, and therefore not a health hazard)” to “A positron-emitting glucose analog (2-[18F]-fluoro-2-deoxy-D-glucose).” Extra double bond above N in guanine residues should be deleted. Adjust J gene subscripts.
3rd
Change “a different N atom” to “C-5”
3rd
In the ribosome cartoon at the bottom of the figure, the tRNA bound in the A site should have AA2 attached, not fMet.
4th
3rd 3rd
3rd 3rd
4th 3rd
1097
Fig. 28-26 and caption
1097 Line 10 Index
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…” In the equation, change “ppGpp” to “(p)ppGpp.” Entries for Chapter 15 (pp. 525-566) were off by one page (525 should be 526, etc.) in the first three printings.
4th
4th 4th
