@article{open840,
          volume = {21},
          number = {1},
           month = {February},
          author = {D Sareen and R Sharma and H S Nandanwar and R M Vohra},
            note = {Copyright of this article belongs to Elsevier Science.},
           title = {Two-step purification of d(-)-specific carbamoylase from Agrobacterium tumefaciens AM 10.},
       publisher = {Elsevier Science},
            year = {2001},
         journal = {Protein expression and purification},
           pages = {170--5},
        keywords = {-Carbamoylase; Agrobacterium; dye affinity; purification},
             url = {http://crdd.osdd.net/open/840/},
        abstract = {A simple, economical and rapid affinity chromatography procedure with red dye as a ligand has been described for the two-step purification of a relatively thermostable d(-)-carbamoylase from the cell-free extract of Agrobacterium tumefaciens AM 10. The enzyme was purified 232-fold to homogeneity with a recovery of 30\% in the presence of 2 mM dithiothreitol. The specific activity of the enzyme was 7.88 U/mg protein. The enzyme is a dimer with a native molecular mass of 67 kDa and a subunit relative molecular mass of 38 kDa. The isoelectric point of the enzyme was found to be 5.83. The K(m) values for N-carbamoyl-dl-methionine and N-carbamoyl-d-phenylglycine were 3.84 and 5.0 mM, respectively.}
}