Purification and characterization of a nicotinamide deamidase released into the growth medium of neuroblastoma in vitro.

@article{Wintzerith1980PurificationAC,
  title={Purification and characterization of a nicotinamide deamidase released into the growth medium of neuroblastoma in vitro.},
  author={Marguerite Wintzerith and Andr{\'e}e Di{\'e}rich and Paul D. Mandel},
  journal={Biochimica et biophysica acta},
  year={1980},
  volume={613 1},
  pages={
          191-202
        }
}
Nicotinamide deamidase (nicotinamide amidohydrolase, EC 3.5.1.19) has been demonstrated in the conditioned growth medium of the M1 clonal cell line of mouse C1300 neuroblastoma. The enzyme has been purified 1200-1500-fold by Sephadex G25, hydroxyapatite, DEAE-cellulose, Sephadex G200 and NAD-Sepharose column chromatographies. The purified protein was characterized by polyacrylamide gel electrophoresis under non-denaturing and denaturing conditions. The apparent molecular weight has been… CONTINUE READING