Characterization of lens cyrstallins and their mRNA from the carp lenses
Resource
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 871 (3): 324-328
Journal
Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology
Pages
324-328
Date Issued
1986
Date
1986
Author(s)
Chiou, Shyh-Horng
Chang, Tschining
Chang, Wen-Chang
Kuo, Jane
Lo, Tung-Bin
Abstract
Crystallins from carp eye lenses have been isolated and characterized by gel permeation chromatography, SDS-gel electrophoresis, immunodiffusion and amino acid analysis. gamma-Crystallin is the most abundant class of crystallins and constitutes over 55% of the total lens cytoplasmic proteins. It is immunologically distinct from the alpha- and beta-crystallins isolated from the same lens and its antiserum shows a very weak cross-reaction to total pig lens antigens. Comparison of the amino acid compositions of carp gamma-crystallin with those of bovine gamma-II, haddock gamma- and squid crystallins indicates that gamma-crystallin from the carp is very closely related to that of the haddock, and probably also related to the invertebrate squid crystallin. In vitro translation of total mRNAs isolated from carp lenses confirms the predominant existence of gamma-crystallin. The genomic characterization of carp crystallin genes should provide some insight into the mechanism of crystallin evolution in general.
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