{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,4]],"date-time":"2025-09-04T13:32:08Z","timestamp":1756992728220},"reference-count":0,"publisher":"Canadian Science Publishing","issue":"4","license":[{"start":{"date-parts":[[1977,4,1]],"date-time":"1977-04-01T00:00:00Z","timestamp":228700800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Can. J. Biochem."],"published-print":{"date-parts":[[1977,4,1]]},"abstract":"<jats:p> The M<jats:sub>1<\/jats:sub> isozyme of pyruvate kinase has been purified from human psoas muscle in a seven-step procedure. Fractionation by ammonium sulfate precipitation, heat treatment, acetone precipitation, diethylaminoethyl cellulose batchwise treatment followed by chromatography on carboxymethyl cellulose and Sephadex G-200 gave a product with a specific activity of 383\u2002U\/mg representing a 294-fold purification with a yield of 11%. The product formed orthorhombic crystals and was homogeneous on polyacrylamide gel electrophoresis with and without sodium dodecyl sulfate, sedimentation velocity, sedimentation equilibrium, and immunodiffusion. The purified enzyme has a molecular weight of 240\u2002700 and has a sedimentation coefficient (s<jats:sub>20<\/jats:sub>,<jats:sub>w<\/jats:sub>) of 10.04\u2002S. It contains four subunits with identical molecular weights of 61\u2002000. No free N-terminal amino acids could be detected. Antibody prepared against the purified human M<jats:sub>1<\/jats:sub> isozyme does not cross-react by immunodiffusion or enzyme inactivation with the human erythrocyte isozyme and in the reverse experiment antibody prepared against human erythrocyte pyruvate kinase does not cross-react with the purified M<jats:sub>1<\/jats:sub> isozyme. The amino acid composition of the M<jats:sub>1<\/jats:sub> isozyme is presented. <\/jats:p>","DOI":"10.1139\/o77-042","type":"journal-article","created":{"date-parts":[[2009,12,21]],"date-time":"2009-12-21T14:47:27Z","timestamp":1261406847000},"page":"301-307","source":"Crossref","is-referenced-by-count":16,"title":["Purification and characterization of human muscle pyruvate kinase"],"prefix":"10.1139","volume":"55","author":[{"given":"Richard N.","family":"Harkins","sequence":"first","affiliation":[]},{"given":"John A.","family":"Black","sequence":"additional","affiliation":[]},{"given":"Marvin B.","family":"Rittenberg","sequence":"additional","affiliation":[]}],"member":"155","container-title":["Canadian Journal of Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nrcresearchpress.com\/doi\/pdf\/10.1139\/o77-042","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,1,5]],"date-time":"2020-01-05T22:52:10Z","timestamp":1578264730000},"score":1,"resource":{"primary":{"URL":"http:\/\/www.nrcresearchpress.com\/doi\/10.1139\/o77-042"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1977,4,1]]},"references-count":0,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1977,4,1]]}},"alternative-id":["10.1139\/o77-042"],"URL":"https:\/\/doi.org\/10.1139\/o77-042","relation":{},"ISSN":["0008-4018"],"issn-type":[{"value":"0008-4018","type":"print"}],"subject":[],"published":{"date-parts":[[1977,4,1]]}}}