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

FEBS Letters

Chen, Shun-Wen¹  Chiou, Shyh-Horng¹  Lo, Tung-Bin¹ 

[1] Institute of Biochemical Sciences, National Taiwan University and Institute of Biological Chemistry, Academia Sinica, PO Box 23-106, Taipei, Taiwan, Republic of China

关键词: Lens crystallin Protein sequence Sequence homology Microheterogeneity Multigene family;   

DOI  :  10.1016/0014-5793(86)81093-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown