Results 171 to 180 of about 38,489 (227)
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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 ...
N O Kaplan
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Stability of dehydrogenases III. malate dehydrogenases
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982Cytoplasmic and mitochondrial malate dehydrogenases from pig and chicken were studied by chemical modification of amino groups, hybridization of immobilization. Determination of thermal stability was used to characterize the different species. Modification of amino groups was found to decrease thermal stability especially when neutralization of the ...
J, Müller, C, Klein
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Glutamate dehydrogenase-malate dehydrogenase complex
Archives of Biochemistry and Biophysics, 1979Abstract Kinetic and Sephadex gel filtration epxeriments indicate that in the presence of palmitoyl-CoA, glutamate dehydrogenase forms a complex with mitochondrial malate dehydrogenase. In this complex, palmitoyl-CoA is bound to glutamate dehydrogenase but is not bound to malate dehydrogenase.
L A, Fahien, E, Kmiotek, L, Smith
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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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Stabilization of halophilic malate dehydrogenase
Journal of Molecular Biology, 1989Malate dehydrogenase from the extreme halophile, Halobacterium marismortui, is stable only in highly concentrated solutions of certain salts. Previous work has established that its physiological environment is saturated in KCl; it remains soluble is saturated NaCl or KCl solutions; also it unfolds in solutions containing less than 2.5 M-NaCl or -KCl ...
G, Zaccai +4 more
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Malate dehydrogenase in leaf peroxisomes
Biochimica et Biophysica Acta (BBA) - Enzymology, 1969Abstract The technique of isopycnic centrifugation of leaf homogenates has allowed a separation of chloroplasts, mitochondria, and peroxisomes according to their respective densities. Chlorophyll, cytochrome c oxidase, and glycolate oxidase, respectively, were used as markers for these organeles. Malate dehydrogenase ( l -malate; NAD oxidoreductase,
R K, Yamazaki, N E, Tolbert
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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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Heterogeneity of supernatant malate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1968Abstract A way was found to demonstrate electrophoretically that the supernatant portion of pig heart malate dehydrogenase ( l -malate:NAD oxidoreductase, EC 1.1.1.37) is heterogeneous. Other pig organs displayed the same pattern of supernatant malate dehydrogenase forms.
R J, Kulick, F W, Barnes
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Cooperativity in the mechanism of malate dehydrogenase
Biochemistry, 1993Cooperativity in the catalytic mechanism of porcine cytoplasmic malate dehydrogenase (sMDH) has been a point of ongoing discussion. Though previous investigations revealed little evidence of cooperativity, chemical modification studies reported by this laboratory demonstrate that binding of cofactor or cofactor plus substrate causes the enzyme's ...
C T, Zimmerle, G M, Alter
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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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