Malate dehydrogenase, inhibition of pig heart supernatant enzyme by iodoacetamide.

Malate dehydrogenase, inhibition of pig heart supernatant enzyme by iodoacetamide.

Pig heart supernatant malate dehydrogenase is alkylated by 250 mM iodoacetamide at 37 degrees C in pH 7.5 Tris/acetate buffer which is 0.05 M with respect to acetate to form enzyme with 1,3-dicarboxamidomethyl histidine, 3-carboxamidomethyl histidine, 1-carboxamidomethyl histidine, carboxamidomethyl cysteine, and carboxamidomethyl methionine. 1,3-Dicarboxamidomethyl histidine forms with a stoic...

Malic dehydrogenase. 8. Large scale purification and properties of supernatant pig heart enzyme.

A reproducible procedure for the large scale purification of pig heart supernatant malate dehydrogenase which yields up to 400 mg of homogeneous protein has been developed. The purity of the isolated enzyme is shown by acrylamide gel electrophoresis over a pH range from 4.9 to 9.2 as well as by detailed analysis of boundary spreading during sedimentation velocity experiments. Three enzymically ...

Physicochemical properties of pig and horse heart mitochondrial malate dehydrogenase.

Kinetic studies on pig heart cytoplasmic malate dehydrogenase.

Kinetic studies on the pig heart cytoplasmic malate dehydrogenase have been performed over a wide range of conditions using the full time course of the reaction and computer simulation to obtain the kinetic parameters. The maximum velocity and Michaelis constants for the oxidation of reduced coenzyme have been determined as a fundtion of pH in 0.05 M phosphate buffer at 15 degrees. At pH 7.5 an...

Multiple forms of supernatant malate dehydrogenase in salmonid fishes.

Salmon generally possess three forms of supernatant malate dehydrogenase whose subunit compositions are indicated by the formulas AA, AB, and BB. Each of the homodimers (AA and BB) has now been purified to homogeneity. The two enzymes are similar in molecular size and in catalytic properties to the supernatant malate dehydrogenases of higher vertebrates; both are catalytically distinct from the...