Abstract
1. 1. Equine erythrocyte hexokinase (ATP: D-hexose 6-phosphotransferase, EC2. 7.I.I) was isolated in a partially-purified preparation by KCl elution from DEAE-Sephadex A-50, ammonium sulfate precipitation and Sephadex G-75 gel filtration. 2. 2. The K m values for glucose and adenosine triphosphate were 0.04 and 0.5 mM respectively. 3. 3. The enzyme was inhibited by 2,3-diphosphoglycerate (DPG) at the in vivo concentration of this glycolytic intermediate. The inhibition of hexokinase by DPG was a function of the Mg 2+ and ATP concentrations. 4. 4. These findings indicate that the low intracellular ATP concentration in the mature erythrocyte of the horse may be the major factor which regulates hexokinase activity in this cell type.
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