[Isolation and some properties of N-acetyl-beta-D-hexosaminidase from Sarcoscipha coccinea].

N-Acetyl-beta-D-hexosaminidase was isolated from the extract of the discomycet Sarcoscipha coccinea and purified 510--550-fold by gel filtration on Sephadex G-200 and by ion-exchange chromatography on KM-Sephadex C-50 and DEAE-Sephadex A-50 or by a combination of hydrophobic and affinity chromatographies. Gel electrophoresis confirmed the homogeneity of the enzyme in both cases. Some properties of purified N-acetyl-beta-D-hexosaminidase (e. g. pH optimum, thermal stability, molecular weight, etc.) were studied. The Michaelis constants and maximal cleavage rates for some substrates were determined. The tissue extract of S. coccinea was found to contain two molecular forms of N-acetyl-beta-D-hexosaminidase. At concentrations of N-acetyl-p-nitrophenyl-beta-D-glucosaminide and D-galactosaminide higher than 0,5 mM the enzyme is inhibited by an excess of the substrate.