Abstract

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 Asp11, Asn2, Thr14, Ser11, Glu19, Gln6, Pro6, Gly19, Ala8, Cys2, Val17, Met6, Ile9, Leu18. Tyr7, Phe5, Lys21, His2, Arg11. 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‐Ile10‐Ile‐Phe‐Val‐Val‐Gly‐Gly‐Pro‐Gly ‐ Ser‐Gly20‐Lys‐Gly‐Thr‐Gln‐Cys‐Glu‐Lys‐Ile‐Val‐Gln30‐Lys‐Tyr‐Gly‐Tyr‐Thr‐His‐Leu‐Ser‐Thr‐Gly40‐Asp‐Leu‐Leu‐Arg‐Ala‐Glu‐Val‐Ser‐Ser‐Gly50‐Ser‐Ala‐Arg‐Gly‐Lys‐Met‐Leu‐Ser‐Glu‐Ile60‐Met‐Glu‐Lys‐Gly‐Gln‐Leu‐Val‐Pro‐Leu‐Glu70‐Thr‐Val‐Leu‐Asp‐Met‐Leu‐Arg‐Asp‐Ala‐Met80‐Val‐Ala‐Lys‐Val‐Asp‐Thr‐Ser‐Lys‐Gly‐Phe90‐Leu‐Ile‐Asp‐Gly‐Tyr‐Pro‐Arg‐Glu‐Val‐Lys100‐Gln‐Gly‐Glu‐Glu‐Phe‐Glu‐Arg‐Lys‐Ile‐Gly110‐Gln‐Pro‐Thr‐Leu‐Leu‐Leu‐Tyr‐Val‐Asp120‐Ala‐Gly‐Pro‐Glu‐Thr‐Met‐Thr‐Lys‐Arg‐Leu‐Leu130‐Lys‐Arg‐Gly‐Glu‐Thr‐Ser‐Gly‐Arg‐Val‐Asp140‐Asp‐Asn‐Glu‐Glu‐Thr‐Ile‐Lys‐Lys‐Arg‐Leu150‐Glu‐Thr‐Tyr‐Tyr‐Lys‐Ala‐Thr‐Glu‐Pro‐Val160‐Ile‐Ala‐Phe‐Tyr‐Glu‐Lys‐Arg‐Gly‐Ile‐Val170‐Arg‐Lys‐Val‐Asn‐Ala‐Glu‐Gly‐Ser‐Val‐Asp180‐Asp‐Val‐Phe‐Ser‐Gln‐Val‐Cys‐Thr‐His‐Leu190‐Asp‐Thr‐Leu‐Lys.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.