Kinetic studies on rabbit-muscle myokinase

Kinetic studies on rabbitmuscle myokinase.

Kinetic studies of rabbit muscle lactate dehydrogenase.

A number of reports have appeared in recent years on the mechanism, i.e. the mode of enzyme and substrate interaction, of anaerobic dehydrogenases. For example, the mechanisms of heart muscle lactate dehydrogenase (1)) yeast alcohol dehydrogenase (2), and ribitol dehydrogenase (3) appear to involve a compulsory sequence of enzyme and substrate interaction leading to one or more kinetically impo...

The purification and properties of rabbit-muscle myokinase.

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Structural Studies on Rabbit Muscle Glycogen Synthase

Limited tryptic digestion of either synthase I or D forms resulted in the appearance of a new glucose 6-phosphate-dependent form which was composed of 75,000 molecular weight subunits. Early in tryptic digestion, an intermediate 78,000 subunit was also observed with both forms of the enzyme. The NH,terminal dipeptide sequence of the 75,000 subunit of both forms was the same as that of the origi...

Adenylate deaminase. Kinetic and binding studies on the rabbit muscle enzyme.

Kinetic studies with adenylate deaminase have been performed by stopped flow methods at 20 degrees C in 0.01 M imidazole/HCl, pH 6.5. The data were analyzed using either the whole time course of the reaction or the initial portion of the full time course. At low KCl concentrations, activation by the product IMP complicates any interpretation. In the presence of 0.15 M KCl, the results are inter...