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Studies on the structure of the calcium dependent atpase from rabbit skeletal muscle sarcoplasmic reticulum



Studies on the structure of the calcium dependent atpase from rabbit skeletal muscle sarcoplasmic reticulum



Archives of Biochemistry & Biophysics 203(2): 780-791



The linear arrangement of the 3 fragments of Ca2+-ATPase from rabbit skeletal muscle sarcoplasmic reticulum with MW of 20,000, 30,000 and 45,000 obtained by limited tryptic hydrolysis was determined by locating the NH2-terminal acetylated methionyl residue of the original peptide in the MW = 20,000 fragment. Since both the MW = 20,000 and 30,000 polypeptides orginate from a MW = 55,000 fragment which is distinct from the MW = 45,000 polypeptide, the sequence of these 3 fragments was determined to be 20,000, 30,000 and 45,000. The MW = 20,000 fragment was further cleaved by cyanogen bromide to yield a MW = 7000 COOH-terminal fragment which is relatively hydrophilic. The NH2-terminal portion is rich in glutamyl residues. The COOH-terminus of the MW = 30,000 fragment was determined by both digestion with carboxypeptidases and cyanogen bromide cleavage. Using the partial amino acid sequence of the Ca2+-ATPase, it was deduced that the active site phosphoaspartyl residue is 154 amino acids from the COOH-terminus of the MW = 30,000 fragment and hence approximately 35,000 MW from the NH2-terminus of the original Ca2+-ATPase molecule. It was shown that the 2 tryptic cleavages of the Ca2+-ATPase generating these large fragments were both single hydrolyses of arginylalanine peptide bonds.

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