The Amino‐Acid Sequence of Porcine Adenylate Kinase from Skeletal Muscle

Adenylate kinase (ATP:AMP phosphotransferase) has been purified 490‐fold from porcine muscle with a final yield of 60 mg/kg muscle. The amino‐acid composition is Asp 11 , Asn 2 , Thr 14 , Ser 11 , Glu 19 , Gln 6 , Pro 6 , Gly 19 , Ala 8 , Cys 2 , Val 17 , Met 6 , Ile 9 , Leu 18 . Tyr 7 , Phe 5 , Lys 21 , His 2 , Arg 11 . The protein molecule is a single polypeptide chain of 194 amino‐acid residues with an acetyl‐methionine at the N‐terminus and a lysine residue at the C‐terminus. Cyanogen bromide cleavage of carboxymethylated adenylate kinase yielded six fragments which were further degraded by using trypsin, chymotrypsin, thermolysin, subtilisin or α‐protease. Sequence data on the resulting peptides are summarized in the present report, full details are given in a supplementary paper which has been deposited at CNRS from where copies can be obtained. The primary structure of porcine adenylate kinase is: Ac‐Met‐Glu‐Glu‐Lys‐Leu‐Lys‐Lys‐Ser‐Lys‐Ile 10 ‐Ile‐Phe‐Val‐Val‐Gly‐Gly‐Pro‐Gly ‐ Ser‐Gly 20 ‐Lys‐Gly‐Thr‐Gln‐Cys‐Glu‐Lys‐Ile‐Val‐Gln 30 ‐Lys‐Tyr‐Gly‐Tyr‐Thr‐His‐Leu‐Ser‐Thr‐Gly 40 ‐Asp‐Leu‐Leu‐Arg‐Ala‐Glu‐Val‐Ser‐Ser‐Gly 50 ‐Ser‐Ala‐Arg‐Gly‐Lys‐Met‐Leu‐Ser‐Glu‐Ile 60 ‐Met‐Glu‐Lys‐Gly‐Gln‐Leu‐Val‐Pro‐Leu‐Glu 70 ‐Thr‐Val‐Leu‐Asp‐Met‐Leu‐Arg‐Asp‐Ala‐Met 80 ‐Val‐Ala‐Lys‐Val‐Asp‐Thr‐Ser‐Lys‐Gly‐Phe 90 ‐Leu‐Ile‐Asp‐Gly‐Tyr‐Pro‐Arg‐Glu‐Val‐Lys 100 ‐Gln‐Gly‐Glu‐Glu‐Phe‐Glu‐Arg‐Lys‐Ile‐Gly 110 ‐Gln‐Pro‐Thr‐Leu‐Leu‐Leu‐Tyr‐Val‐Asp 120 ‐Ala‐Gly‐Pro‐Glu‐Thr‐Met‐Thr‐Lys‐Arg‐Leu‐Leu 130 ‐Lys‐Arg‐Gly‐Glu‐Thr‐Ser‐Gly‐Arg‐Val‐Asp 140 ‐Asp‐Asn‐Glu‐Glu‐Thr‐Ile‐Lys‐Lys‐Arg‐Leu 150 ‐Glu‐Thr‐Tyr‐Tyr‐Lys‐Ala‐Thr‐Glu‐Pro‐Val 160 ‐Ile‐Ala‐Phe‐Tyr‐Glu‐Lys‐Arg‐Gly‐Ile‐Val 170 ‐Arg‐Lys‐Val‐Asn‐Ala‐Glu‐Gly‐Ser‐Val‐Asp 180 ‐Asp‐Val‐Phe‐Ser‐Gln‐Val‐Cys‐Thr‐His‐Leu 190 ‐Asp‐Thr‐Leu‐Lys.