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.
D000118:Acetylglucosaminidase / Q000302:isolation & purification / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D012831:Bombyx / Q000201:enzymology*; D005944:Glucosamine / Q000032:analysis; D006023:Glycoproteins / Q000302:isolation & purification; D006458:Hemolymph; D006596:Hexosaminidases / Q000378:metabolism; D006601:Hexoses / Q000032:analysis; D008970:Molecular Weight
D000596:Amino Acids; D006023:Glycoproteins; D006601:Hexoses; D006596:Hexosaminidases; D000118:Acetylglucosaminidase; D005944:Glucosamine