Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3.

@article{Schr1986PurificationAC,
  title={Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3.},
  author={H. P. Sch{\"a}r and W. L. C. Holzmann and Gerardo M. Ramos Tombo and Oreste Ghisalba},
  journal={European journal of biochemistry},
  year={1986},
  volume={158 3},
  pages={
          469-75
        }
}
The N,N-dimethylformamide-hydrolyzing enzyme (DMFase) from Pseudomonas DMF 3/3 has been purified to apparent electrophoretic homogeneity with an overall 49-fold purification, a 24% yield and a final specific activity of 1.98 mumol N,N-dimethylformamide (DMF) hydrolyzed min-1 (mg protein)-1. The native DMFase has a relative molecular mass of 250 000 and is composed of two light-chain (Mr = 15 000) and two heavy-chain (Mr = 105 000) subunits. The stability of DMFase is optimal at pH values above… 

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