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N-acetyl-aspartate amidohydrolase: purification and properties.
Authors:A F D'Adamo  J Peisach  G Manner  C T Weiler
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 Km 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.
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