The Amino‐Acid Sequence of the Most Acidic Major Parvalbumin from Frog Muscle

Abstract

The primary structure of the most acidic (pI - 4.50) of the two major parvalbumins from frog (Rana esculenta) has been determined from a study of its trypsic peptides and of overlapping peptides generated by limited trypsic digestion, chymotrypsic digestion and N-bromosuccinimide cleavage of the protein. The amino acid sequence so obtained is considered in comparison with those known for other parvalbumins and for rabbit troponin-C.