Biochem J. 1972 Jul; 128(4): 971–974.
Abstract
The amino acid sequence of a snail cytochrome c has been determined. The molecule consists of a single polypeptide chain of 104 residues, and is homologous with other mitochondrial cytochromes c. Unlike the cytochromes c from vertebrates, there is no acetyl blocking group at the N-terminus. A change in an otherwise invariant position has been observed in position 87. Comparison with amino acid sequences of cytochromes c from other sources indicates that the point of divergence of the molluscs and the vertebrates in evolutionary time was 720 million years ago. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50009 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1972), 126, 5.
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Selected References
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Articles from Biochemical Journal are provided here courtesy of The Biochemical Society
Procedure: 1. Refer to the following table of amino acid sequences of cytochrome-c, compare the
amino acid sequences of the following pairs of organisms by encircling the portions of
the
sequences where they differ. For each pair, count the total number of differing
amino acids
human and chimpanzee
b. human and rhesus monkey
c horse and monkey
d. chicken and turkey
e rattlesnake and fruit fly
Answer:
human and chimpanzee amino-1 percentage difference 1.2% human and Rhesus Monkey amino-8 percentage difference 93% horse and donkey amino-21 percentage difference 0% chicken and turkey amino-2 percentage difference 92%
Explanation:
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