| Literature DB >> 5419 |
Abstract
Two forms (Peak A and Peak B) of thymidine kinase [EC 2.7.1.75] from regenerating rat liver cytosol were resolved and partially purified by Deae-cellulose chromatography. Both fractions were identical with respect to their substrate requirement, pH optima, metal requirements, and molecular weight, as judged by their sedimentation in sucrose density gradient centrifugation. Peak B differed from Peak A in heat sensitivity, inhibition by dCTP and Km for thymidine and ATP. Peak B enzyme was the only enzyme found in normal adult liver and Peak A enzyme was the form increasing predominantly in regenerating liver.Entities:
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Year: 1975 PMID: 5419 DOI: 10.1093/oxfordjournals.jbchem.a131019
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387