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Primary structure of zeta-crystallin protein from guinea pig. Its similarity to the enzyme alcohol dehydrogenase.

作者信息

Borrás T, Rodokanaki A

机构信息

Laboratory of Molecular Mechanisms of Ocular Diseases, National Eye Institute, National Institutes of Health, Bethesda, MD 20892.

出版信息

Lens Eye Toxic Res. 1989;6(4):795-805.

PMID:2487283
Abstract

The primary structure of zeta-crystallin, a guinea pig lens specific protein, was obtained by cloning the copy of its mRNA from a 0-1 week old cDNA lens library. The protein is 328 amino acids long and 34% of its secondary structure appears in alpha-helical conformation. Comparison of the zeta-crystallin sequence with the sequences of the protein data base bank, revealed the similarity of this lens protein to the enzymes of the long-chain zinc-containing alcohol dehydrogenase family.

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