title: The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans.
abstract: N-Methylglutamate dehydrogenase, purified to a specific activity of 0.29 unit/mg of protein, gave one band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, corresponding to a molecular weight of 130 000. Enzyme-Triton complexes were found to have a partial specific volume of 0.73 cm3/g, suggesting that the protein binds less than 0.1 g of Triton/g of protein. A molecular weight for the intact enzyme in the presence of 1% (w/v) Triton X-100 of 550 000 suggested that the enzyme may be a tetramer.
mesh_terms: D055598:Chemical Phenomena; D002621:Chemistry; D005971:Glutamates; D008970:Molecular Weight; D010089:Oxidoreductases, N-Demethylating / Q000302:isolation & purification*; D011549:Pseudomonas / Q000201:enzymology*
chemical_list: D005971:Glutamates; D010089:Oxidoreductases, N-Demethylating; C021577:N-methylglutamate dehydrogenase