Purification, characterization, and localization of aspartoacylase from bovine brain.

摘要: Canavan disease, an autosomal recessive disorder, is characterized biochemically by N-acetylaspartic aciduria and aspartoacylase (N-acyl-L-aspartate amidohydrolase; EC 3.5.1.15) deficiency. However, the role of acid in brain metabolism unknown. Aspartoacylase has been purified to apparent homogeneity with a specific activity approximately 19,000-20,000 nmol aspartate released/mg protein. The native enzyme 58-kDa monomer. enhanced divalent cations, nonionic detergents, dithiothreitol. Low levels dithiothreitol or beta-mercaptoethanol are required for stability. Km 8.5 x 10(-4) M Vmax 43,000 nmol/min/mg Inhibition glycyl-L-aspartate amino derivatives D-aspartic suggests that carbon backbone substrate primarily involved its interaction active site blocked group essential catalytic aspartoacylase. Biochemical immunocytochemical studies revealed localized white matter, whereas concentration threefold higher gray matter than matter. Our so far indicate conserved across species during evolution suggest significant normal biology.