Results 181 to 190 of about 38,489 (227)
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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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Inheritance of malate dehydrogenase nulls in soybean
Biochemical Genetics, 1992Three chlorophyll-deficient mutants (CD-1, CD-2, and CD-3), derived from the progeny of independent germinal revertants from the w4-mutable soybean line [Glycine max (L.) Merrill], were characterized genetically. Electrophoretic analyses indicated that these lines lacked two of three mitochondrial malate dehydrogenase isozymes (MDH-).
B R, Hedges, R G, Palmer
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Purification and properties of drosophila malate dehydrogenases
Biochimica et Biophysica Acta (BBA) - Enzymology, 1970Abstract The supernatant and mitochondrial forms of malate dehydrogenase ( l -malate:NAD oxidoreductase, EC 1.1.1.37) have been purified from Drosophila virilis Texmelucan (1801.1). The mitochondrial enzyme was judged homogeneous by ultra-centrifugal and electrophoretic criteria and has an s 20,w of 4.0 S.
M S, McReynolds, G B, Kitto
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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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The purification and properties of Neurospora malate dehydrogenase
Archives of Biochemistry and Biophysics, 1965Abstract A procedure is described for the isolation of Neurospora malate dehydrogenase. The isolated protein represents 0.2–0.4% of the total extractable protein and is over 90% pure as evidenced by sedimentation velocity, sedimentation equilibrium, and N-terminal amino acid analyses.
K D, MUNKRES, F M, RICHARDS
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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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Two malate dehydrogenases in Methanobacterium thermoautotrophicum
Archives of Microbiology, 1998Methanobacterium thermoautotrophicum (strain Marburg) was found to contain two malate dehydrogenases, which were partially purified and characterized. One was specific for NAD+ and catalyzed the dehydrogenation of malate at approximately one-third of the rate of oxalacetate reduction, and the other could equally well use NAD+ and NADP+ as coenzyme and ...
Thompson, H. +3 more
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Binding of mitochondrial malate dehydrogenase to mitoplasts
Canadian Journal of Biochemistry, 1979The binding of 14C-labelled bovine and porcine malate dehydrogenase (EC 1.1.1.37) to rat liver mitochondria and mitoplasts was examined. The bovine enzyme was found to associate nonspecifically with isolated mitochondria and sonicated mitoplasts.
P M, Strasberg +3 more
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Effects of ultrasound on catalase and malate dehydrogenase
The Journal of the Acoustical Society of America, 1980Catalase and malate dehydrogenase (MDH) were subjected to the sound field produced by a transversely oscillating wire driven at 20 kHz. Catalase was not inactivated under any conditions of sonication whereas MDH inactivation increased exponentially with the duration of sonication and depended upon the initial enzyme concentration.
H A, Kashkooli, J A, Rooney, R, Roxby
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Polymorphism of malate dehydrogenase in Ascaris suum
Biochemical Genetics, 1970Starch gel electrophoresis of homogenates prepared from adult Ascaris suum revealed polymorphism for the number, staining intensity, and electrophoretic mobility of the cytoplasmic isozymes of malate dehydrogenase (MDH). Five different variant isozymic patterns were found among the 2160 worms surveyed.
D S, Zee, H, Isensee, W H, Zinkham
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