A study of the coenzyme-binding characteristics of rabbit muscle L-glycerol 3-phosphate dehydrogenase.
1. The binding of NAD(+) and NADH to glycerol 3-phosphate dehydrogenase was studied in the pH range 6.0-9.0 at 25 degrees C and in the temperature range 16-43 degrees C at pH7.0. 2. The second-order velocity constants for the combination of NADH with the enzyme in the pH range 6.0-9.0 and for the combination of NAD(+) with the enzyme at pH6.0 were determined. 3. The velocity constant for the dissociation of the enzyme-NAD(+) complex at pH6.0 was measured.
D000818:Animals; D001665:Binding Sites; D002021:Buffers; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004492:Edetic Acid; D005453:Fluorescence; D005993:Glycerolphosphate Dehydrogenase; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008722:Methods; D009132:Muscles / Q000201:enzymology*; D009243:NAD; D010710:Phosphates; D011485:Protein Binding; D011817:Rabbits; D013696:Temperature
D002021:Buffers; D010710:Phosphates; D009243:NAD; D004492:Edetic Acid; D005993:Glycerolphosphate Dehydrogenase