Insect haemolymph exo-beta-N-acetylglucosaminidase from Bombyx mori. Purification and properties.

Haemolymph exo-beta-N-acetylglucosaminidase from the silkworm, Bombyx mori was purified to homogeneity as shown by disc-electrophoresis and ultracentrifugation. It appeared to be composed of two identical subunits of 61 000 molecular weight, which were obtained by sodium dodecyl sulfate-electrophoresis. The purified enzyme was capable of hydrolyzing phenyl N-acetyl-beta-D-glucosaminide, phenyl N-acetyl-beta-D-galactosaminide and N N'-diacetylchitobiose in the relative ratios 100:20:3. The enzyme was found to be a glycoprotein containing about 4% of neutral sugar.