Primary structure of beta s-crystallin from human lens.
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.
Zarina
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S
H.E.J. Research Institute of Chemistry, University of Karachi, Pakistan.
Abbasi
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A
Zaidi
Z H
ZH
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
D003459:Crystallins; D038222:gamma-Crystallins; C077648:CRYGS protein, human