title: Isolation and characterization of the CNBr peptides from the proteolytically derived N-terminal fragment of ovine opsin.
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.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D003488:Cyanogen Bromide; D005136:Eye Proteins; D010446:Peptide Fragments / Q000302:isolation & purification; D017299:Rod Opsins; D012756:Sheep
chemical_list: D000596:Amino Acids; D005136:Eye Proteins; D010446:Peptide Fragments; D017299:Rod Opsins; D003488:Cyanogen Bromide