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Purification and Properties of Pig-Heart Hexokinase.

Authors :
Easterby, John S.
O'Brien, Michael J.
Source :
European Journal of Biochemistry. 1973, Vol. 38 Issue 2, p201-211. 11p.
Publication Year :
1973

Abstract

Hexokinase has been purified from pig heart to a specific activity of 80 units/mg. The enzyme has an s20 of 5.11 ± 0.15S and a molecular weight of 97000. Dodecyl-sulphate-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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
38
Issue :
2
Database :
Academic Search Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
13659269
Full Text :
https://doi.org/10.1111/j.1432-1033.1973.tb03051.x