Purification and characterization of Neurospora crassa N-acetyl galactosaminoglycan deacetylase.
1. N-Acetyl galactosaminoglycan deacetylase was purified from Neurospora mycelium 215-fold in 25% yield to electrophoretic homogeneity. A single band corresponding to a molecular weight of 76,000 was obtained by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. 2. The enzyme activity had pH optima at pH 5.0 and 9.0. Sodium molybdate, 2 mM, stimulated enzyme activity 4-fold at pH 5.0 but had no effect at pH 9.0. Cupric ion, 1 mM, inhibited activity by more than 85% at pH 5.0 and 9.0. The Km of the enzymatic reactions was 16 microM on the basis of the concentration of N-acetylgalactosamine. 3. This enzyme may be involved in determining the properties of the hyphal apex of the colonial form of Neurospora crassa and thus could play a role in morphogenetic regulation.
D000581:Amidohydrolases / Q000302:isolation & purification* / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009024:Morphogenesis; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology* / Q000254:growth & development
D003470:Culture Media; D002265:Carboxylic Ester Hydrolases; C036914:N-acetylgalactosaminoglycan deacetylase; D000581:Amidohydrolases