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. 1976 Feb 1;153(2):363–373. doi: 10.1042/bj1530363

The purification in high yield and characterization of rat hepatic glucokinase.

M J Holroyde, M B Allen, A C Storer, A S Warsy, J M Chesher, I P Trayer, A Cornish-Bowden, D G Walker
PMCID: PMC1172582  PMID: 1275894

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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