The amino-terminal sequences of four major carp γ-crystallin polypeptides and their homology with frog and calf γ-crystallins
Resource
FEBS Letters 209 (1): 107-110
Journal
FEBS Letters
Pages
107-110
Date Issued
1986
Date
1986
Author(s)
Chiou, Shyh-Horng
Chen, Shun-Wen
Lo, Tung-Bin
Abstract
Four major gamma-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 gamma-crystallin polypeptides. Comparison of the carp N-terminal sequences with those of mammalian and amphibian gamma-crystallins also showed a high degree of homology present in their N-terminal segments despite the dissimilarity of amino acid compositions of fish gamma-crystallins to those of higher classes of vertebrates. The distinct yet closely-related partial sequences of carp gamma-crystallins could account for the profound microheterogeneity detected in the characterization of carp crystallins, suggesting the presence of a multigene family for gamma-crystallin in the lowest class of vertebrates, i.e. the fish.
SDGs
File(s)![Thumbnail Image]()
Loading...
Name
03.pdf
Size
388.69 KB
Format
Adobe PDF
Checksum
(MD5):1fd7eb39d3036b24e23a14a017f79ca1