The amino-terminal sequences of four major carp γ-crystallin polypeptides and their homology with frog and calf γ-crystallins

Four major γ-crystallin subfractions have been isolated from the carp ( Cyprinus carpio) and their N-terminal sequences determined by Edman protein sequencing. Extensive homologies indicative of close relatedness in their primary structure were found in these four γ-crystallin polypeptides. Comparis...

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Published inFEBS letters Vol. 209; no. 1; pp. 107 - 110
Main Authors Chiou, Shyh-Horng, Chen, Shun-Wen, Lo, Tung-Bin
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 01.12.1986
Elsevier
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Summary:Four major γ-crystallin subfractions have been isolated from the carp ( Cyprinus carpio) and their N-terminal sequences determined by Edman protein sequencing. Extensive homologies indicative of close relatedness in their primary structure were found in these four γ-crystallin polypeptides. Comparison of the carp N-terminal sequences with those of mammalian and amphibian γ-crystallins also showed a high degree of homology present in their N-terminal segments despite the dissimilarity of amino acid compositions of fish γ-crystallins to those of higher classes of vertebrates. The distinct yet closely-related partial sequences of carp γ-crystallins could account for the profound microheterogeneity detected in the characterization of carp crystallins, suggesting the presence of a multigene family for γ-crystallin in the lowest class of vertebrates, i.e. the fish.
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ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)81093-6