{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,3,30]],"date-time":"2022-03-30T03:05:23Z","timestamp":1648609523354},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"4","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1973,8,1]]},"abstract":"<jats:p>The bacteriophage P1 modification enzyme was purified 1400-fold from induced lysogens of a thermoinducible mutant of bacteriophage P1. The most purified fraction, when analysed by polyacrylamide-gel electrophoresis in sodium dodecyl sulphate, showed two principal stained bands. The two bands co-sedimented in a glycerol gradient with the modification activity, at a rate which, when compared with the rate of sedimentation of marker proteins, corresponds to a sedimentation coefficient in water of 6S. The mobilities of the bands on sodium dodecyl sulphate\u2013polyacrylamide-gel electrophoresis corresponded to polypeptides of molecular weight 70000 and 45000 and they were present in equimolar amounts. It was concluded that the 6S species of the enzyme is a dimer of unlike subunits.<\/jats:p>","DOI":"10.1042\/bj1330629","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T19:49:22Z","timestamp":1439236162000},"page":"629-633","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["The deoxyribonucleic acid modification enzyme of bacteriophage P1. Subunit structure"],"prefix":"10.1042","volume":"133","author":[{"given":"Jeremy P.","family":"Brockes","sequence":"first","affiliation":[{"name":"Medical Research Council Molecular Genetics Unit, Department of Molecular Biology, University of Edinburgh, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, U.K."}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/133\/4\/629\/561128\/bj1330629.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/133\/4\/629\/561128\/bj1330629.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T15:48:11Z","timestamp":1637941691000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/133\/4\/629\/8618\/The-deoxyribonucleic-acid-modification-enzyme-of"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1973,8,1]]},"references-count":0,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1973,8,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1330629","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1973,8,1]]}}}