Parvalbumin from Rabbit Muscle. Isolation and Primary Structure

Abstract
A parvalbumin, with its characteristic low MW (.apprxeq. 12,000), acidic isoelectric point (.apprxeq. 5.5), UV spectrum (maximum 259 nm) and Ca2+-binding capacity (2 mol/mol protein) was isolated from rabbit (Oryctolagus cuniculus) muscle. Its primary structure was determined from a study of its tryptic peptides and of overlapping peptides generated by limited tryptic digestion and by chymotryptic and thermolytic digestions of the protein. The amino acid sequence so obtained is considered in comparison with those known for other parvalbumins and for rabbit troponin C.