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- W2228305244 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." @default.
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- W2228305244 date "1983-06-01" @default.
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- W2228305244 title "Isolation and characterization of the CNBr peptides from the proteolytically derived <i>N</i>-terminal fragment of ovine opsin" @default.
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- W2228305244 doi "https://doi.org/10.1042/bj2110661" @default.
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