Purification and Properties of Pig‐Heart Hexokinase
Open Access
- 1 October 1973
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 38 (2) , 201-211
- https://doi.org/10.1111/j.1432-1033.1973.tb03051.x
Abstract
Hexokinase has been purified from pig heart to a specific activity of 80 units/mg.The enzyme has an s20 of 5.11 ± 0.15 S and a molecular weight of 97000. Dodecylsulphate‐polyacrylamide electrophoresis and maleylation of the enzyme each suggest that it contains a single polypeptide chain. Amino‐acid analysis reveals similarities between the compositions of heart and brain hexokinases. Steady‐state kinetic investigations at sub‐optimal substrate concentrations are consistent with a mechanism in which at least one of the substrates is in equilibrium with its enzyme · substrate complex.Keywords
This publication has 37 references indexed in Scilit:
- Purification and Subunit Interactions of Yeast HexokinaseEuropean Journal of Biochemistry, 1972
- The polypeptide chain molecular weight of a mammalian hexokinaseFEBS Letters, 1971
- Purification and characterization of wheat germ hexokinasesFEBS Letters, 1971
- Immunoglobulin biosynthesis: IV. Carbohydrate attachment to immunoglobulin subunitsJournal of Molecular Biology, 1970
- The melecular weight of the undegraded polypeptide chain of yeast hexokinaseBiochemical and Biophysical Research Communications, 1970
- Effect of sodium dodecyl sulphate on human plasma low density lipoproteinsFEBS Letters, 1970
- TISSUE DISTRIBUTION AND PHYSIOLOGICAL SIGNIFICANCE OF MULTIPLE FORMS OF HEXOKINASEAnnals of the New York Academy of Sciences, 1968
- On the mechanism of the dissociation of haemoglobinJournal of Molecular Biology, 1967
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- The Relationship between Michaelis Constants, Maximum Velocities and the Equilibrium Constant for an Enzyme-catalyzed ReactionJournal of the American Chemical Society, 1953