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Journal of Molecular Evolution

, Volume 1, Issue 1, pp 74–83 | Cite as

Hominoid evolution as judged by fibrinopeptide structures

  • R. F. Doolittle
  • G. L. Wooding
  • Y. Lin
  • M. Riley
Article

Summary

The fibrinopeptides A and B from gorilla, organgutan and siamang have been characterized, thereby completing a study of all six extant hominoids. The gorilla peptides were identical with the corresponding fibrinopeptides previously reported for human and chimpanzee. The orangutan peptide A was also identical with the human-chimpanzee-gorilla type A, but its fibrinopeptide B had two amino acid differences. The siamang A peptide differed from the others in one of its sixteen residues, but its peptide B was identical with the orangutan B. A cladogram based on the fibrinopeptide sequences of all six hominoids indicates that five amino acid replacements and one deletion can account for the evolution of present day sequences. It was also possible to deduce the amino acid sequence of the fibrinopeptides of the common ancestor of Old World monkeys and hominoids.

Key-words

Hominoids Fibrinopeptides 

Abbreviations Used

PITC

phenylisothiocyanate

DNS

dimethylaminonaphthalene sulfonyl-

PCA

pyrrolidone carboxylic acid

ASP

aspartic acid

ASN

asparagine

THR

threonine

SER

serine

GLU

glutamic acid

GLN

glutamine

GLY

glycine

ALA

alanine

VAL

valine, ILE isoleucine

LEU

leucine

PHE

phenylalanine

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Copyright information

© Springer-Verlag 1971

Authors and Affiliations

  • R. F. Doolittle
    • 1
  • G. L. Wooding
    • 1
  • Y. Lin
    • 1
  • M. Riley
    • 1
  1. 1.Department of Chemistry, Revelle CollegeUniversity of CaliforniaLa JollaUSA

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