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. 1983 Jun 1;211(3):661–670. doi: 10.1042/bj2110661

Isolation and characterization of the CNBr peptides from the proteolytically derived N-terminal fragment of ovine opsin.

M Brett, J B Findlay
PMCID: PMC1154411  PMID: 6224479

Abstract

Ovine rhodopsin may be cleaved in situ by Staphylococcus aureus V8 proteinase into two membrane-bound fragments designated V8-L (27 000 mol.wt.) and V8-S (12 000 mol.wt.). After purification of the proteolysed complex by affinity chromatography in detergent using concanavalin A immobilized on Sepharose 4B, the two polypeptide fragments may be separated by gel-permeation chromatography on Sephadex LH-60. Digestion of the N-terminal-derived V8-L fragment with CNBr in 70% (v/v) trifluoroacetic acid resulted in a peptide mixture that could be fractionated by procedures involving gel-permeation chromatography in organic and aqueous solvents and the use of differential solubility. The complete or partial sequences of all ten peptides are reported.

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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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