抄録
The liver of common octopus Octopus vulgaris contained extremely high activity of β-N-acetyl-hexosaminidase which is useful for structural and functional studies of complex carbohydrates. Asimple procedure has been devised for the isolation of β-N-acetylhexosaminidase from the liver inan electrophoretically homogeneous form. The procedure involved heat treatment at 68°C for 20min, Sephadex G-200 gel filtration, and CM-Sephadex C-50 chromatography. The purified enzyme was sufficiently free from other glycosidases and proteases. The molecular weight of the enzyme was estimated to be 147, 000 by Sephadex G-200 gel filtration. The enzyme exhibited the optimum pH at pH 5.0 and was stable between pH 4 and 8. For p-nitrophenyl β-N-acetylgluco-saminide, Km was 0.63mM and Vmax was 192μmol/min•mg.
