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J. Biochem, 1984, Vol. 95, No. 6 1603-1615
© 1984 Japanese Biochemical Society

research-article

Amino Acid Sequence of {alpha} Chain of Sarcoplasmic Calcium Binding Protein Obtained from Shrimp Tail Muscle

Takashi TAKAGI and Kazuhiko KONISHI

Biological Institute, Faculty of Science, Tohoku University Sendai, Miyagi 980

The isotypes of sarcoplasmic Ca2+ binding protein (SCP) were purified from shrimp tail muscle. SCP exists in a dimeric form. One sample of shrimp contained only {alpha}A chain, whereas another contained {alpha}B and ß chains, and a heterodimer of {alpha}Bß which was not analyzed precisely. The amino acid sequences of the two a chains were determined. The two a chains are composed of 190 and 192 amino acid residues, respectively. The sequences of the two {alpha} chains differed in only four amino acids out of 192 residues. The sequences indicate that the {alpha} chain has three Ca2+-binding sites which are common to EF-hand type Ca2+-binding protein. In the absence of added Ca2+ and Mg2+, the amounts of bound Ca2+ in {alpha}A, {alpha}B, and ß chains were 3.0, 3.3, and 2.4 mol/22,000 g protein, respectively. Thus, it is suggested that all three isotypes of shrimp SCP have three Ca2+-binding sites which have high affinity to Ca2+. The sequence homology of shrimp SCP with other EF-hand type Ca2+-binding proteins is very low. The protein having the greatest homology with this SCP was cod parvalbumin; the sequence homology is 18%.


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