Open AccessPurification and Properties of Pig‐Heart Hexokinase
Author(s) -
Easterby John S.,
O'Brien Michael J.
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb03051.x
Subject(s) - hexokinase , enzyme , substrate (aquarium) , biochemistry , polyacrylamide gel electrophoresis , chemistry , steady state (chemistry) , electrophoresis , chromatography , biology , glycolysis , organic chemistry , ecology
Hexokinase has been purified from pig heart to a specific activity of 80 units/mg. The enzyme has an s 20 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.