Comparison of the amino acid sequences of tissue-specific parvalbumins from chicken muscle and thymus and possible evolutionary significance

Biochem Biophys Res Commun. 1991 Nov 27;181(1):226-31. doi: 10.1016/s0006-291x(05)81406-8.


Chicken leg muscle parvalbumin was digested with cyanogen bromide or trypsin or trypsin after citraconylation. Peptides isolated by reverse phase HPLC at pH 7.0 were subjected to acid hydrolysis and amino acid analysis and, in some cases, sequencing. The chicken muscle parvalbumin amino acid sequence has ca. 80% sequence identity with alpha-type parvalbumins from mammalian (rabbit, human and rat) muscle. By contrast, the chicken thymus parvalbumin ("avian thymic hormone") sequence is very similar to reptile (turtle, salamander and frog) muscle beta-type parvalbumins. We hypothesize that the evolutionary appearance of the warm-blooded reptiles was accompanied by recruitment of the beta parvalbumin isozyme for promotion of lymphocyte maturation.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Evolution*
  • Chickens
  • Humans
  • Mammals
  • Molecular Sequence Data
  • Muscles / physiology*
  • Parvalbumins / chemistry
  • Parvalbumins / genetics*
  • Reptiles
  • Sequence Homology, Nucleic Acid
  • Thymus Gland / physiology*


  • Parvalbumins