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[Purification and partial sequence of a hydrophobic polypeptide from BNPS-skatole cleaved bovine rhodopsin]
Abstract:
Rhodopsin isolated from outer segments of cattle retinas was cleaved at tryptophan residues by the BNPS-skatole. One of the polypeptides obtained S 5 (molecular weight about 12,000) of hydrophobic nature was isolated and the sequence of its 50 first residues revealed 60% of hydrophobic AA.