Lactate dehydrogenase associated with the mitochondrial fraction and with a mitochondrial inhibitor--I. Enzyme binding to the mitochondrial fraction.
Rabbit skeletal muscle mitochondrial fraction shows LDH activity (212 +/- 43 U/g pellet). The majority of the mitochondrial enzyme was solubilized by washing with 0.15 M NaCl, pH 6, or by ultrasonic treatment in the same medium. It was also solubilized on increasing the ionic strength and the pH of the medium. Cytosoluble LDH was observed to bind in vitro to the particulate fraction and the enzyme bound was a sigmoidal function of the amount of soluble enzyme added. The bound enzyme is less active than the soluble one. Kinetically, active mitochondrial fraction or in vitro bound enzyme showed non-hyperbolic behavior which is different from the bi-bi sequential-ordered type mechanism of the soluble enzyme.
D000818:Animals; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008931:Mitochondria, Muscle / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology*; D009994:Osmolar Concentration; D011817:Rabbits; D012995:Solubility; D013347:Subcellular Fractions / Q000201:enzymology; D013696:Temperature
D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase