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Dissociation of mitochondrial malate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984The kinetics of the dissociation reaction under acidic conditions of the dimeric pig and chicken mitochondrial malate dehydrogenases (EC 1.1.1.37) have been studied. The dissociation of the pig enzyme is completely reversible. The pK for dissociation determined by light-scattering measurements agrees within experimental error with the pK value of 5.25 ...
J, Muller, H, Gorisch, L J, Parkhurst
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Purification of Chlorella Malate Dehydrogenase
Preparative Biochemistry, 1972Abstract Our prior investigation of Chlorella malate dehydrogenase (MDH) revealed supernatant and particulate isoenzymes which were immunologically, chromatographically, and electro-phoretically distinct. By means of ammonium sulfate fractionation and column chromatography a crystalline preparation of the particulate isoenzyme, specific activity of ...
F E, Cole, L, Naron
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Mitochondrial Malate Dehydrogenase: Reversible Denaturation Studies
Science, 1968The malate dehydrogenase isoenzymes from the mitochondria of chicken hearts have been partially resolved into separate pools. Reversible denaturation, in concentrated guanidine hydrochloride, does not change the isoenzyme distribution in each pool.
A N, Schechter, C J, Epstein
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Genetic alteration of Neurospora malate dehydrogenase
Archives of Biochemistry and Biophysics, 1965Abstract Purified malate dehydrogenases of wild-type Neurospora and two genetically nonlinked malate mutants of Neurospora were compared. The mutant enzymes differed significantly from those of the wild-type in stability, turnover number, pH optima, sedimentation constant, molecular weight, amino acid composition, and electrophoretic mobility.
K D, MUNKRES, F M, RICHARDS
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Properties of mitochondrial malate dehydrogenases
Biochimica et Biophysica Acta, 1962Abstract The malate dehydrogenases of the mitochondria of ox heart, rat liver and rabbit kidney and those extracted from acetone-dried powders of horse, pig and pigeon hearts have been purified and compared by a number of criteria. In substrate and coenzyme specificities, in the values for some Michaelis constants, and in their behaviour during ...
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Starch-gel electrophoresis of malate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963Abstract Malate dehydrogenase preparations were subjected to electrophoresis on starch gel at pH 7.0. Purified preparations of mitochondrial malate dehydrogenase were shown to exist in up to six separable forms on the gel. The distribution pattern of these forms was not influenced by the age of the tissue of origin, the purification procedures used ...
C J, THORNE, L I, GROSSMAN, N O, KAPLAN
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Kinetic determination of malate dehydrogenase isozymes
Journal of Molecular and Cellular Cardiology, 1978Abstract These studies determine the levels of malate dehydrogenase isoenzymes in cardiac muscle by a steady state kinetic method which depends on the differential inhibition of these isoenzyme forms by high concentrations of oxaloacetate. This inhibition is similar to that exhibited by lactate dehydrogenase in the presence of high concentrations of ...
L H, Bernstein, M B, Grisham
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Evolution of Malate Dehydrogenase in Birds
Science, 1966Heart extracts from over 100 species of birds were subjected to starch-gel electrophoresis at p H 7. The "supernatant" form of malate dehydrogenase, an enzyme present in every extract, was then located on the gels by a specific staining method.
G B, Kitto, A C, Wilson
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Multiple forms of mitochondrial malate dehydrogenases
Biochemical and Biophysical Research Communications, 1966Chromatography on carboxymethyl cellulose to obtain fractions containing predominantly single bands of malate ...
G B, Kitto +3 more
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Subunit dissociation of mitochondrial malate dehydrogenase
Biochemistry, 1976Fluorescence polarization studies of porcine mitochondrial malate dehydrogenase labeled with fluorescein isothiocyanate or fluorescamine indicated a concentration-dependent dissociation of the dimeric molecule with a KD OF 2 X 10(7) N at pH 8.0. These results were confirmed by the concentration dependence of the stability of the enzyme at elevated ...
J D, Shore, S K, Chakrabarti
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