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Primary structure of beta s-crystallin from human lens
S Zarina1, A Abbasi, Z H Zaidi
1H.E.J. Research Institute of Chemistry, University of Karachi, Pakistan.
The Biochemical Journal
|October 15, 1992
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.