Haemolymph exo-β-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-β-d-glucosaminide, phenyl N-acetyl-β-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. © 1976.
Kimura, S. (1976). Insect haemolymph exo-β-N-acetylglucosaminidase from Bombyx Mori Purification and properties. BBA - Protein Structure, 446(2), 399–406. https://doi.org/10.1016/0005-2795(76)90006-4