Results 301 to 310 of about 369,761 (340)
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1975
Publisher Summary The oxidation of L-malate in most living organisms is catalyzed by two distinct types of pyridine nucleotide-dependent enzymes. In one case the principal product is oxaloacetate, while in the other it is pyruvate and CO 2 .
Leonard J. Banaszak, Ralph A. Bradshaw
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Publisher Summary The oxidation of L-malate in most living organisms is catalyzed by two distinct types of pyridine nucleotide-dependent enzymes. In one case the principal product is oxaloacetate, while in the other it is pyruvate and CO 2 .
Leonard J. Banaszak, Ralph A. Bradshaw
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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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Polymorphism of malate dehydrogenase in Ascaris suum [PDF]
Biochemical Genetics, 1970 Starch 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.
H. Isensee +2 more
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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.
F.M. Richards, Kenneth D. Munkres
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Flow-injection determination of malate with immobilized malate dehydrogenase
Analytica Chimica Acta, 1989Abstract Malate dehydrogenase (MDH) is immobilized chemically on controlled-pore glass and used on-line in a glass minicolumn (25×2.5 mm i.d.). Malate solution passes through the minicolumn of immobilized MDH and the NADH formed is monitored spectrophotometrically from 9 × 10-−4 down to 7 × 10−6 M (36 ng in 40 μl) at 50 samples h−1.
Ala'ddin M. Almuiabed, Alan Townshend
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O-GlcNAcylation promotes pancreatic tumor growth by regulating malate dehydrogenase 1
Nature Chemical Biology, 2022Qian Zhu +11 more
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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 ...
Larry H. Bernstein +3 more
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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.
Kenneth D. Munkres, F.M. Richards
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Malate Dehydrogenase and Other Enzymes
Functional Plant Biology, 1976The activity and some properties of NADH malate dehydrogenase in extracts of marine plants was investigated. Activity was detected in 24 species examined and average rates [in µmol min-1 (mg chlorophyll)-1] in the major groups were: Cyanophyta, 47; Chlorophyta, 74; Phaeophyta, 35; Rhodophyta, 69; and Anthophyta, 150.
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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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