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Developmental and aging patterns of pyruvate kinase (PK) isozymes (PK 1, PK 2, PK 3, and PK 4) from rat liver, kidney, heart, and skeletal muscle were studied by electrophoretic, chromatographic and immunochemical techniques. During the first 2 weeks of postnatal life a decline of total PK activity occurred in liver, kidney, and heart followed by an(More)
The kinetic properties of lactate dehydrogenase (LDH) isozymes have been determined at high enzyme concentrations. Spectrophotofluorometric assays revealed that the extent of substrate inhibition of LDH-1 and LDH-5 depends on enzyme concentration. At high enzyme concentrations, in the range of those that exist in most mammalian cells, no inhibition by(More)
By competition with lactate dehydrogenase (LDH) for nicotinamide adenine dinucleotide (NAD), commonly occurring intracellular proteins, such as glyceraldehyde-3-phosphate dehydrogenase, malate dehydrogenase, and albumin, can protect LDH-1 and LDH-5 from inhibition and ternary complex formation with NAD and pyruvate. The existence of intracellular proteins(More)
Rates of formation and dissociation of an abortive ternary complex between lactate dehydrogenase isozymes from various mammalian tissues, NADf, and pyruvate were studied utilizing stopped-flow spectrofluorometry. Formation of the complex was accompanied by a decrease in protein fluorescence at 340 rnp and a loss of lactate dehydrogenase activity. Rates of(More)
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