| Literature DB >> 1275894 |
M J Holroyde, M B Allen, A C Storer, A S Warsy, J M Chesher, I P Trayer, A Cornish-Bowden, D G Walker.
Abstract
A new improved procedure for the purification of rat hepatic glucokinase (ATP-d-glucose 6-phosphotransferase, EC 2.7.1.2) is given. A key step is affinity chromatography on Sepharose-N-(6-aminohexanoyl)-2-amino-2-deoxy-d-glucopyranose. A homogeneous enzyme, specific activity 150 units/mg of protein, is obtained in about 40% yield. The molecular weight of the pure enzyme was determined by several procedures. In particular, sedimentation-equilibrium studies under a variety of conditions indicate a molecular weight of 48000 and no evidence for dimerization; reports in the literature of other values are discussed in the light of this evidence on the pure enzyme. The amino acid composition suggests that hepatic glucokinase is closely related to rat brain hexokinase and also the wheat "light" hexokinases.Entities:
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Year: 1976 PMID： 1275894 PMCID： PMC1172582 DOI： 10.1042/bj1530363
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857