title: Primary structure of zeta-crystallin protein from guinea pig. Its similarity to the enzyme alcohol dehydrogenase.
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.
authors.affiliation: Laboratory of Molecular Mechanisms of Ocular Diseases, National Eye Institute, National Institutes of Health, Bethesda, MD 20892.
authors.forename: T
authors.initials: T
authors.lastname: Borrás
authors.forename: A
authors.initials: A
authors.lastname: Rodokanaki
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003459:Crystallins / Q000737:chemistry* / Q000235:genetics; D004247:DNA; D015723:Gene Library; D006168:Guinea Pigs; D008969:Molecular Sequence Data; D016415:Sequence Alignment
chemical_list: D003459:Crystallins; D004247:DNA; D000426:Alcohol Dehydrogenase