Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
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Question
Chapter 24, Problem 33P
Interpretation Introduction
Interpretation:
Some organisms use glutamate dehydrogenase pathway for glutamate synthesis.
Concept introduction:
Glutamate dehydrogenase (GDH) is an enzyme, which is present in microbes and eukaryotic mitochondria. Its function is to catalyze the interconversion of glutamate and alpha-ketoglutarate. the ammonia produced during this process is used in the urea cycle. In the brain, liver, kidney, and pancreas high levels of GDH are found.
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Electrophoresis
Macmillan Learning
Chymotrypsin is a protease with a molecular mass of 25.6 kDa. The figure shows a stained SDS polyacrylamide gel with a
single band in lane I and three bands of lower molecular weight in lane 2. Lane I contains a preparation of chymotrypsin and
lane 2 contains chymotrypsin pre-treated with performic acid.
1
2
Why does performic acid treatment of chymotrypsin generate three bands in lane 2?
°
Chymotrypsin self-digests on the carboxyl-terminal side of phenylalanine, tryptophan, or tyrosine residues.
The three peptides are impurities in the original chymotrypsin sample.
Performic acid cleaves proteins on the carboxyl-terminal side of lysine and arginine residues.
Performic acid cleaves the disulfide bonds holding together the three subunits of chymotrypsin.
Correct Answer
Extracts from the bacterium Bacillus brevis contain a peptide with antibiotic properties. This peptide forms complexes with
metal ions and seems to disrupt ion transport across the cell membranes of other bacterial species, leading to bacterial death.
The structure of the peptide has been determined from a series of observations.
(a) Complete acid hydrolysis of the peptide, followed by amino acid analysis, yielded equimolar amounts of Leu, Orn, Phe, Pro,
and Val. Orn is ornithine, an amino acid not present in proteins but present in some peptides. Orn has the structure
H
'H,N-CH,
-
CH2 CH2 CH2 -
C - COO-
NH,
(b) The molecular weight of the peptide is approximately 1,200 Da.
(c) The peptide failed to undergo hydrolysis when treated with the enzyme carboxypeptidase. This enzyme catalyzes the
hydrolysis of the carboxyl-terminal residue of a polypeptide unless the residue is Pro or the peptide does not contain a free
carboxyl group.
(d) Treatment of the intact peptide with…
At a pH equal to the isoelectric point (pl) of alanine, the net charge of alanine is zero. Two structures can be drawn that have a
net charge of zero, but the predominant form of alanine at its pl is zwitterionic.
CH3
H,N
CH3
**
H¸N-C
H
Zwitterionic
H
Uncharged
OH
Select statements that explain why alanine is predominantly zwitterionic at its pl.
pk of alanine's amino group is more than its pl.
pk of alanine's carboxyl group is more than its pl.
PK of alanine's carboxyl group is less than its pl.
pk of alanine's amino group is less than its pl.
Correct Answer
What fraction of alanine is in the completely uncharged form at its pl?
1 in 2.2 × 107
1 in 1.6 × 10²
1 in 4680
1 in 9460
Chapter 24 Solutions
Biochemistry
Ch. 24 - Prob. 1PCh. 24 - Prob. 2PCh. 24 - Prob. 3PCh. 24 - Prob. 4PCh. 24 - Prob. 5PCh. 24 - Prob. 6PCh. 24 - Prob. 7PCh. 24 - Prob. 8PCh. 24 - Prob. 9PCh. 24 - Prob. 10P
Ch. 24 - Prob. 11PCh. 24 - Prob. 12PCh. 24 - Prob. 13PCh. 24 - Prob. 14PCh. 24 - Prob. 15PCh. 24 - Prob. 16PCh. 24 - Prob. 17PCh. 24 - Prob. 18PCh. 24 - Prob. 19PCh. 24 - Prob. 20PCh. 24 - Prob. 21PCh. 24 - Prob. 22PCh. 24 - Prob. 23PCh. 24 - Prob. 24PCh. 24 - Prob. 25PCh. 24 - Prob. 26PCh. 24 - Prob. 27PCh. 24 - Prob. 28PCh. 24 - Prob. 29PCh. 24 - Prob. 30PCh. 24 - Prob. 31PCh. 24 - Prob. 32PCh. 24 - Prob. 33PCh. 24 - Prob. 34P
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