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. 1966 May;99(2):266–274. doi: 10.1042/bj0990266

Purification and properties of adenosine 5′-triphosphate–D-glucose 6-phosphotransferase from rat liver

M J Parry 1, D G Walker 1
PMCID: PMC1264993  PMID: 5944237

Abstract

1. An 870-fold purification of glucokinase from rat liver is described which involves ammonium sulphate fractionation and the use of DEAE-Sephadex, DEAE-cellulose and polyacrylamide columns. 2. The preparation is free of any interfering enzymes and has a specific activity of 8μmoles/min./mg. of protein. 3. Glucokinase catalyses the phosphorylation of glucose, mannose and 2-deoxyglucose. 4. The enzyme is inhibited by high concentrations of glucose 6-phosphate only; ADP is an inhibitor whose effect depends on the Mg2+ concentration. 5. The properties of glucokinase are compared briefly with those of other phosphotransferases.

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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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