Results 271 to 280 of about 7,790 (296)
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Polarography of Cadmium Malate Complexes
Talanta, 1973The electrode reduction reaction of cadmium malate complexes at various pH values and ligand concentrations has been studied. At pH < pK(1) the complex Cd(H(2)A), log K = 0.57, exists. At pH > pK(2) Cd(A(2-))(n) species exist, log beta(1) = 1.9, log beta(2) = 2.8 log beta(3) = 3.4. At intermediate pH the complex Cd(HA) exists.
C.M. Gupta, S.C. Khurana
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[19] Quantitation of malate, oxaloacetate, and malate dehydrogenase
1978Publisher Summary This chapter reviews the quantitation of l-malate and oxaloacetate using malate dehydrogenase and by monitoring the change in level of NADH with dehydrogenaseluciferase complex derived from Photobacterium fischeri. Malate dehydrogenase may be measured using the same approach, but with saturating levels of malate and excess NAD ...
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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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Malate transport into heart mitochondria
Journal of Molecular and Cellular Cardiology, 1975Abstract The oxidation of l -Malate to carbon dioxide was employed as a measure of malate transport into mitochondria. Conditions of incubation were optimized with regard to osmolarity, pH, phosphate concentration, and substrate concentrations.
William J. Reddy, Stanley B. Digerness
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Purification and properties of malate synthetase
Biochimica et Biophysica Acta, 1960Abstract Procedures are described for the purification of malate synthetase from baker's yeast and from glycollate-grown Pseudomonas ovalis Chester. The properties of the enzymes are closely similar: both re optimally active at pH 8.5 but that from yeast shows greater activity below this pH than that from Ps. ovalis .
G.H. Dixon +2 more
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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 ...
Helmut Görisch +3 more
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Triammine cobalt(III)-L-malate. Malate ion as a tridentate ligand
Polyhedron, 1991Abstract The crystal structure of the title compound has been determined from single crystal X-ray diffraction data. There is little angle strain in the complex which has two carboxylate ions and one alkoxide ion bound to cobalt(III). These conclusions agree with IR, CD and NMR spectral data except that 1H coupling constants show that the ...
Bunel Torrealba, Sergio +5 more
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The malate synthase gene of cucumber
Plant Molecular Biology, 1989The complete sequences of a full-length cDNA clone and a genomic clone encoding the Cucumis sativus glyoxysomal enzyme malate synthase, have been determined. The sequences have enabled us to identify putative control regions at the 5' end of the gene, three introns, and possible alternative polyadenylation sites at the 3' end.
Ian A. Graham +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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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 ...
Nina Borochov +4 more
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