Abstract
The interaction of rabbit muscle lactate dehydrogenase and 2,4,5,7-tetraiodofluorescein has been studied spectrophotometrically and in the temperature-jump apparatus. The perturbation of the dye absorption spectrum after binding to the enzyme has been used to determine that the enzyme has approximately six equivalent high affinity sites for the dye, with an intrinsic dissociation constant of 13 μM. High concentrations of NAD + or NADH decrease but do not eliminate dye binding, suggesting that two of these sites are not associated with the active sites. Temperature-jump studies show the presence of two relaxation processes in solutions of dye and enzyme, one of which is eliminated by high concentrations of NADH or NAD +, while the other persists in the presence of the coenzymes. The faster process, which is subject to NADH inhibition, indicates that the lactate dehydrogenase-dye complex isomerizes after dye binding.
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