Malate Dehydrogenases of Pisum sativum

Comparative Enzymology of the Glyceraldehyde 3-Phosphate Dehydrogenases from Pisum sativum.

Glyceraldehyde 3-phosphate dehydrogenases (EC 1.2.1.12 and 1.2.1.13) have been purified from the seed, root, etiolated, and green shoot of peas (Pisum sativum). These enzymes are tetramers of 140,000 daltons, with subunits of 35,000 daltons. The enzymes differ in isoelectric point. The seed enzyme has a pI of 5.1, and the root enzyme has a pI of 4.5. The cytoplasmic enzyme from etiolated shoots...

The isoperoxidases of Pisum sativum.

The heterogeneity of the peroxidases in peas was examined by starch gel electrophoresis. Comparisons were made between tall and dwarf cultivars and among organ systems developed in light and darkness. Isoperoxidase bands could be grouped as cathodic, anodic and near-neutral (at pH 9.0) types. The cathodic set stained well with guaiacol oxidation products whereas some anodic bands reacted prefer...

Malate dehydrogenases--structure and function.

Malate dehydrogenases (MDH, L-malate:NAD oxidoreductase, EC 1.1.1.37), catalyze the NAD/NADH-dependent interconversion of the substrates malate and oxaloacetate. This reaction plays a key part in the malate/aspartate shuttle across the mitochondrial membrane, and in the tricarboxylic acid cycle within the mitochondrial matrix. They are homodimeric molecules in most organisms, including all euka...

DNA methylase from Pisum sativum.

DNA methylase activity was detected in nuclei from pea shoots. The enzyme can only be extracted by low-salt treatment if the nuclei are pretreated with micrococcal nuclease. Only a single enzyme was detected, and it was purified to a specific activity of 1620 units/mg of protein. It has an Mr of 160,000 on gel filtration and SDS/PAGE. Pea DNA methylase methylates cytosine in all four dinucleoti...

Concerning artificial crossing in Pisum sativum.