Bacterial lactate dehydrogenases

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The lactate dehydrogenases of hemopoietic cells.

By W. H. STARKWEATHER, H. H. SPENCER AND H. K. ScriocH M AMMALIAN LACTATE DEHYDROGENASE ( LDH ) can be separated into five active fractions.’4 The production of electrophoretic extremes, LDH-1 (H4 ) and LDH-5 ( M4 ), is controlled by the action of two genes.5’#{176}The intermediate fractions ( LDH-2, LDH-3, LDH-4 ) are considered hybrid forms of LDH-1 and LDH-5.5’” Assuming that the hybrids are...

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Subunit hybridization of higher plant lactate dehydrogenases

developed a procedure, based on the affinity of all three enzymes for Cibacron Blue 3GA, which allows their simultaneous purification from a cell extract. E. coli K 12, EMG-2 was grown, harvested and disrupted as described by Miller & Stadtman (1972). After treatment with 1% (w/v) streptomycin sulphate, the cell extract was subjected to ammonium sulphate fractionation. The protein fraction prec...

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Biochemical properties of trypanosomatid lactate dehydrogenases.

Lactate dehydrogenase (LDH, E.C.1.1.1.27) was found in supernatant (cytoplasmic enzyme) fractions of the trypanosomatid flagellates Trypanosoma conorhini and Crithidia fasciculata if 10 mm cysteine was present in the homogenizing medium. The T. conorhini LDH activity with pyruvate as substrate was increased 35% if 5 mm cysteine was also included in reaction mixtures. K(m) values for the T. cono...

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Membrane-bound lactate dehydrogenases and mandelate dehydrogenases of Acinetobacter calcoaceticus. Purification and properties.

Procedures were developed for the optimal solubilization of D-lactate dehydrogenase, D-mandelate dehydrogenase, L-lactate dehydrogenase and L-mandelate dehydrogenase from wall + membrane fractions of Acinetobacter calcoaceticus. D-Lactate dehydrogenase and D-mandelate dehydrogenase were co-eluted on gel filtration, as were L-lactate dehydrogenase and L-mandelate dehydrogenase. All four enzymes ...

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Membrane-bound lactate dehydrogenases and mandelate dehydrogenases of Acinetobacter calcoaceticus. Location and regulation of expression.

Acinetobacter calcoaceticus possesses an L(+)-lactate dehydrogenase and a D(-)-lactate dehydrogenase. Results of experiments in which enzyme activities were measured after growth of bacteria in different media indicated that the two enzymes were co-ordinately induced by either enantiomer of lactate but not by pyruvate, and repressed by succinate or L-glutamate. The two lactate dehydrogenases ha...

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ژورنال

عنوان ژورنال: Microbiological Reviews

سال: 1980

ISSN: 0146-0749

DOI: 10.1128/mr.44.1.106-139.1980