A spectrophotometric method of measuring the unnatural (—)-tartrate-dehydrating activity of fumarate hydratase was described. The ratio of this activity to the original fumarate-hydrating activity was measured with various crystalline preparations and was constant, provided that the buffer solution used was the same. The ratio of the two activities remained constant despite the inactivation of the enzyme by heat. It was constant also during inactivation by urea and after reactivation by dialysis. By disc electrophoresis the crystalline preparations were separated into one main fraction and several faint subsidiary fractions. Enzymatic activities were found only in the main fraction.
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Nakamura et al. (1968) studied this question.
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