The nicotinamide deamidase of rabbit liver microsomes has been solubilized by the autolytic extraction of microsomal acetone powders. The enzyme has been partially purified and the products of the reaction have been characterized. An inhibitory material associated with the microsomes was largely removed in the preparation of the acetone powder. The nature of the interaction of the enzyme with the naturally occurring inhibitor was found to be very complex, primarily involving changes in Vmax and a shift in pH optimum from pH 8.5 to 8.9 to pH 7.5 to 7.9. The enzyme was also inhibited by detergents and thyroxine.
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Kirchner et al. (1966) studied this question.
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