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. 1992 Oct 15;287(Pt 2):375–381. doi: 10.1042/bj2870375

Primary structure of beta s-crystallin from human lens.

S Zarina 1, A Abbasi 1, Z H Zaidi 1
PMCID: PMC1133175  PMID: 1445197

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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