Sheep liver beta-N-acetylhexosaminidase: partial purification, characterization and photodynamic inactivation.
Sheep liver beta-N-acetylhexosaminidase was purified over 20-fold by conventional methods. The enzyme possessed activity against both p-nitrophenly-beta-D-N-acetylglucosaminide and p-nitrophenyl-beta-D-N-acetylgalactosaminide as substrates. On the basis of a variety of physical and chemical analyses including pH stability, substrate inhibition studies and photodynamic inactivation, it was concluded that both the beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase activities reside within the same molecule.
D000116:Acetylgalactosamine / Q000378:metabolism; D000118:Acetylglucosaminidase / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D004355:Drug Stability; D006596:Hexosaminidases / Q000302:isolation & purification* / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008027:Light; D008099:Liver / Q000201:enzymology*; D012756:Sheep; D013379:Substrate Specificity; D048828:beta-N-Acetyl-Galactosaminidase; D001619:beta-N-Acetylhexosaminidases
D006596:Hexosaminidases; D000118:Acetylglucosaminidase; D001619:beta-N-Acetylhexosaminidases; D048828:beta-N-Acetyl-Galactosaminidase; D000116:Acetylgalactosamine