Purification, crystallization, and properties of D-ribose isomerase from Mycobacterium smegmatis.

@article{Izumori1975PurificationCA,
  title={Purification, crystallization, and properties of D-ribose isomerase from Mycobacterium smegmatis.},
  author={K Izumori and A W Rees and Alan D Elbein},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 20},
  pages={8085-7}
}
D-Ribose isomerase, which catalyzes the conversion of D-ribose to D-ribulose, was purified from extracts of Mycobacterium smegmatis grown on D-ribose. The purified enzyme crystalized as hexagonal plates from a 44% solution of ammonium sulfate. The enzyme was homogenous by disc gel electrophoresis and ultracentrifugal analysis. The molecular weight of the enzyme was between 145,000 and 174,000 by sedimentation equilibrium analysis. Its sedimentation constant of 8.7 S indicates it is globular. On… CONTINUE READING