title: Homology of delta crystallin and argininosuccinate lyase.
abstract: 1. Delta crystallin, a major lens protein characteristic of birds and reptiles, is homologous to argininosuccinate lyase; 57% of the residues in chicken delta crystallin and human lyase are identical. 2. Even more similar (62% identical residues) to the human lyase is the sequence translated from the presumably inactive delta-2 gene of the delta crystallin locus. 3. As both delta crystallin and lyase are synthesized in birds only during the embryonic and juvenile stages, the persistence of delta crystallin in the adult lens appears to be paedomorphic. 4. Possible correlations of the origins of delta crystallin with other events in sauropsid evolution are proposed.
authors.affiliation: National Biomedical Research Foundation, Georgetown University Medical Center, Washington, D.C. 20007.
authors.forename: L S
authors.initials: LS
authors.lastname: Yeh
authors.forename: A
authors.initials: A
authors.lastname: Elzanowski
authors.forename: L T
authors.initials: LT
authors.lastname: Hunt
authors.forename: W C
authors.initials: WC
authors.lastname: Barker
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001123:Argininosuccinate Lyase / Q000032:analysis*; D002645:Chickens; D003459:Crystallins / Q000032:analysis*; D006801:Humans; D008190:Lyases / Q000032:analysis*; D008969:Molecular Sequence Data; D012016:Reference Values; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012689:Sequence Homology, Nucleic Acid
chemical_list: D003459:Crystallins; D008190:Lyases; D001123:Argininosuccinate Lyase