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.
Research Article| November 01 1977
The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans
Biochem J (1977) 167 (2): 509–512.
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
C W Bamforth, P J Large; The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans. Biochem J 1 November 1977; 167 (2): 509–512. doi: https://doi.org/10.1042/bj1670509
Download citation file: