title: Primary structure of beta s-crystallin from human lens.
abstract: The complete primary structure of beta s-crystallin from human lens is reported. The sequence was elucidated by automatic Edman degradation of tryptic and CNBr peptides. The blocked N-terminal dipeptide was identified by fast-atom-bombardment mass spectroscopy. The sequence comparison with other members of crystallin family reveals a closer relationship to human gamma-crystallin (53% identity) than with beta A3/A1 crystallin (37% identity). The structure, evolutionary characteristics and role of beta s-crystallin in lens are discussed.
authors.affiliation: H.E.J. Research Institute of Chemistry, University of Karachi, Pakistan.
authors.forename: S
authors.initials: S
authors.lastname: Zarina
authors.forename: A
authors.initials: A
authors.lastname: Abbasi
authors.forename: Z H
authors.initials: ZH
authors.lastname: Zaidi
mesh_terms: D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003459:Crystallins / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D038222:gamma-Crystallins
chemical_list: D003459:Crystallins; D038222:gamma-Crystallins; C077648:CRYGS protein, human