抄録
Three β-N-acetylhexosaminidases [EC 3.2.1.52] and one β-galactosidase [EC 3.2.1, 23] were purified from the culture filtrate of Streptococcus 6646 group K by a combination of column chromatographies on p-aminophenyl β-D-thiogalactopyranoside-substituted Sepharose and N-(p-aminophenyl)oxamic acid-substituted Sepharose.
These β-N-acetylhexosaminidases showed optimal activities between pH 5.0 and 5.5 and could hydrolyze synthetic and glycopeptidic substrates. Glycolipids such as GM2, asialo-GM2, and globoside I were not susceptible to these β-hexosaminidases.
β-Galactosidase, which was purified more than 11, 000-fold, had a substrate spe-cificity rather similar to that of β-galactosidase from E. coli. This enzyme was inhibited by EDTA and activated by Mn2+, Ca2+, and Mg2+.
Problems pertinent to the application of affinity chromatography to the purification of glycosidases are also discussed.
