<i>N</i>‐ACETYL‐ASPARTATE AMIDOHYDROLASE: PURIFICATION AND PROPERTIES¹

Abstract

Abstract— The enzyme in rat brain responsible for the de‐acetylation of N ‐acetyl‐aspartic acid has been partially purified. In contrast to the enzyme from hog kidney which is stable at 70°C, it rapidly denatures above 57°C. The rat brain enzyme has the same K m for its substrate and the same solubility in ammonium sulphate solution as the hog kidney enzyme. Results of migration on starch gel electro‐phoreses and isoelectric focusing indicate a pI for the amidohydrolase of 5.1. A variety of potential substrates, modulators, and inhibitors have been examined.