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 in | FEBS letters Vol. 209; no. 1; pp. 107 - 110 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
01.12.1986
Elsevier |
Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(86)81093-6 |