Comparison of the amino acid sequences of tissue-specific parvalbumins from chicken muscle and thymus and possible evolutionary significance.
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.
Brewer
J M
JM
Department of Biochemistry, University of Georgia, Athens 30602.
Arnold
J
J
Beach
G G
GG
Ragland
W L
WL
Wunderlich
J K
JK
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002645:Chickens; D006801:Humans; D008322:Mammals; D008969:Molecular Sequence Data; D009132:Muscles / Q000502:physiology*; D010320:Parvalbumins / Q000737:chemistry / Q000235:genetics*; D012104:Reptiles; D012689:Sequence Homology, Nucleic Acid; D013950:Thymus Gland / Q000502:physiology*
D010320:Parvalbumins