Purification and characterization of allantoate amidohydrolase from Bacillus fastidiosus.

Abstract

Allantoate amidohydrolase from Bacillus fastidiosus was purified 170-fold to homogeneity as judged by isoelectric focusing and nondenaturing and sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular mass was estimated to be 128 kDa. The enzyme appeared to be a homodimer with a subunit molecular mass of 66 kDa. The enzyme has an… (More)

Topics

Cite this paper

@article{Xu1995PurificationAC, title={Purification and characterization of allantoate amidohydrolase from Bacillus fastidiosus.}, author={Zh. Y. Xu and F E de Windt and Chris van der Drift}, journal={Archives of biochemistry and biophysics}, year={1995}, volume={324 1}, pages={99-104} }