{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,9]],"date-time":"2026-05-09T03:25:29Z","timestamp":1778297129049,"version":"3.51.4"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1973,9,1]]},"abstract":"<jats:p>1. The low-molecular-weight components of myosin from rabbit skeletal muscle migrated as four bands on polyacrylamide-gel electrophoresis in 8m-urea but only as three in systems containing sodium dodecyl sulphate. The two bands of intermediate mobility in 8m-urea (Ml2 and Ml3) had identical mobilities in sodium dodecyl sulphate. 2. The isolation of pure samples of all four low-molecular-weight components by DEAE-Sephadex chromatography is described. 3. The amino acid compositions of components Ml2 and Ml3 were identical. Further analyses showed the presence of 1 mol of phosphate\/18500g of component Ml2 and less than 10% of this amount in component Ml3. Neither light component contained ribose. 4. Alkaline phosphatase from Escherichia coli converted component Ml2 into Ml3. Incubation with crude preparations of phosphorylase b kinase or protein kinase in the presence of ATP converted component Ml3 into Ml2. 5. Phosphorylation of component Ml3 with the kinases isolated from skeletal muscle and [\u03b3-32P]ATP gave incorporation of 32P only into component Ml2 whether whole myosin or separated low-molecular-weight components were used. 6. High-voltage electrophoresis at pH6.5 and pH1.8 of a chymotryptic digest of 32P-labelled component Ml2 yielded one major radioactive peptide containing serine phosphate. 7. The amino acid sequence of this peptide was shown to be: Arg-Ala-Ala-Ala-Glu-Gly-Gly-(Ser,Ser(P))-Asn-Val-Phe. This sequence shows no obvious similarity to the site phosphorylated in the conversion of phosphorylase b into phosphorylase a by phosphorylase b kinase. 8. Evidence suggests that in vivo all the 18500-molecular-weight light chain is in the phosphorylated form. The extent of dephosphorylation that occurred during myosin extraction depended on the conditions employed.<\/jats:p>","DOI":"10.1042\/bj1350151","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T19:50:41Z","timestamp":1439236241000},"page":"151-164","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":225,"title":["A phosphorylated light-chain component of myosin from skeletal muscle"],"prefix":"10.1042","volume":"135","author":[{"given":"W. T.","family":"Perrie","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Birmingham, Birmingham B15 2TT, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L. B.","family":"Smillie","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Birmingham, Birmingham B15 2TT, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S. V.","family":"Perry","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Birmingham, Birmingham B15 2TT, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/135\/1\/151\/561642\/bj1350151.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/135\/1\/151\/561642\/bj1350151.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T15:49:59Z","timestamp":1637941799000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/135\/1\/151\/8742\/A-phosphorylated-light-chain-component-of-myosin"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1973,9,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1973,9,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1350151","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1973,9,1]]}}}