Abstract
The chapter describes two methods for the determination of the activity of soluble succinate dehydrogenase with artificial electrons acceptors. The first method, a manometric one with Phenazine Methyl Sulfate (PMS), is modified for spectrophotometric use. The rates obtained with the spectrophotometric modification are not proportional with the enzyme concentration. However, when a suitable control lacking succinate is used, the rates are closely proportional. The second method, which uses K 3 Fe(CN) 6 as acceptor, is more convenient as a routine assay. The method of determination of the reconstitution activity of a soluble, purified succinate dehydrogenase preparation is also described. The purification procedure described comprises of 2 parts: preparation of cytochrome c-deficient heart muscle preparation; preparation of the soluble enzyme. The enzyme is very unstable at room temperature even when kept under N 2 . Under all conditions, the reconstitution activity declines faster than the activity with PMS and K 3 Fe(CN)6. The reconstitution activity is fairly stable on storage under liquid N∼; the activity with hydrogen acceptors is also stable under these conditions.
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