Crystallins from carp eye lenses have been isolated and characterized by gel permeation chromatography, SDS-gel electrophoresis, immunodiffusion and amino acid analysis. γ-Crystallin is the most abundant class of crystallins and constitutes over 55% of the total lens cytoplasmic proteins. It is immunologically distinct from the α- and β-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 γ-crystallin with those of bovine γ-II, haddock γ- and squid crystallins indicates that γ-crystallin from the carp is very closely related to that of the haddock, and probably also related to the invertebrate squid cytstalline. In vitro translation of total mRNAs isolated from carp lenses confirms the predominant existence of γ-crystallin. The genomic characterization of carp crystallin genes should provide some insight into the mechanism of crystallin evolution in general.
|頁（從 - 到）||324-328|
|期刊||Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular|
|出版狀態||已發佈 - 六月 23 1986|
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