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






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

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

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.


Accession: 006522122



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