| Literature DB >> 1445197 |
S Zarina1, A Abbasi, Z H Zaidi.
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.Entities:
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Year: 1992 PMID: 1445197 PMCID: PMC1133175 DOI: 10.1042/bj2870375
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857