Effect of various NaCI treatments (0, 50, 100, 200 and 300 mM) at different growth and development stages (tillering, boot swollen, flowering and anthesis) of two wheat cultivars  on the kinetic activity and PAGE electrophoretic pattern of leaf malate dehydrogenase was studied under greenhouse conditions. Ghods was salt-sensitive and Boolani was salt-tolerant. In general, in response to salinti...

accurate protein function prediction is an important subject in bioinformatics, especially wheresequentially and structurally similar proteins have different functions. malate dehydrogenaseand l-lactate dehydrogenase are two evolutionary related enzymes, which exist in a widevariety of organisms. these enzymes are sequentially and structurally similar and sharecommon active site residues, spati...

The interactions between pig heart citrate synthase and mitochondrial malate dehydrogenase or cytosolic malate dehydrogenase were studied using the frontal analysis method of gel filtration and by precipitation in polyethylene glycol. This method showed that an interaction between citrate synthase and mitochondrial malate dehydrogenase occurred but no interaction between citrate synthase and cy...

The interactions between pig heart citrate synthase and mitochondrial malate dehydrogenase or cytosolic malate dehydrogenase were studied using the frontal analysis method of gel filtration and by precipitation in polyethylene glycol. This method showed that an interaction between citrate synthase and mitochondrial malate dehydrogenase occurred but no interaction between citrate synthase and cy...

MALATE OXIDATION IN PLANT MITOCHONDRIA PROCEEDS THROUGH THE ACTIVITIES OF TWO ENZYMES: a malate dehydrogenase and a NAD(+)-dependent malic enzyme. In cauliflower, mitochondria malate oxidation via malate dehydrogenase is rotenone- and cyanide-sensitive. Addition of exogenous NAD(+) stimulates the oxidation of malate via malic enzyme and generates an electron flux that is both rotenone- and cyan...

In vitro refolding of pig mitochondrial malate dehydrogenase is investigated in the presence and absence of Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES). The refolded yields of active malate dehydrogenase are increased almost 3-fold in the presence of groEL, groES, Mg2+/ATP and K+ ions. Chaperonin-assisted refolding of malate dehydrogenase does not have an absolute requirement f...

The citric acid cycle enzyme malate dehydrogenase was purified to homogeneity from the nonsulfur purple bacteria Rhodobacter capsulatus, Rhodospirillum rubrum, Rhodomicrobium vannielii, and Rhodocyclus purpureus. Malate dehydrogenase was purified from each species by either a single- or a two-step protocol: triazine dye affinity chromatography was the key step in purification of malate dehydrog...

In a previous study, we reported the apparent similarity between a low resolution electron density map of mitochondrial malate dehydrogenase and a model of cytoplasmic malate dehydrogenase (Roderick, S. L., and Banaszak, L. J. (1983) J. Biol. Chem. 258, 11636-11642). We have since determined the polypeptide chain conformation and coenzyme binding site of crystalline porcine heart mitochondrial ...

Electrophoretic survey of malate dehydrogenase (EC 1.1.1.37) in Opuntia basilaris showed intraspecific polymorphism. Further experiments with microbody malate dehydrogenase-specific antiserum suggest that the polymorphism occurs in microbody malate dehydrogenase independent of the soluble and mitochondrial forms. The pattern of polymorphism is one expected from a two-allele Mendelian system.