Effects of arginine phosphate and octopine on glycolytic enzyme activities fromSepia officinalis mantle muscle
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Effects of arginine phosphate, arginine, and octopine as modulators of enzyme activity were tested on several partially purified glycolytic enzymes fromSepia officinalis mantle muscle.
Arginine phosphate, at concentrations within its physiological range in resting muscle, was found to be an inhibitor of hexokinase, phosphofructokinase, α-glycerophosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, and pyruvate kinase.
Octopine, the glycolytic end product of mantle muscle, activated pyruvate kinase and phosphoglucomutase but inhibited hexokinase and phosphofructokinase. Arginine affected only one enzyme, slightly inhibiting phosphoglycerate kinase.
The effects of arginine phosphate and octopine were indicated to be direct effects on the glycolytic enzymes themselves as the purification procedures used removed any potential artifact-producing, contaminating enzymes.
The potential roles of arginine phosphate and octopine in the regulation of mantle muscle metabolism in resting versus active muscle are discussed.
KeywordsEnzyme Arginine Hexokinase Pyruvate Kinase Purification Procedure
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