The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans
- 1 November 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 167 (2) , 509-512
- https://doi.org/10.1042/bj1670509
Abstract
N-Methylglutamate dehydrogenase, purified to a specific activity of 0.29 U/mg of protein, gave 1 band on sodium dodecyl sulfate/polyacrylamide-gel electrophoresis, corresponding to a MW of 130,000. Enzyme-Triton complexes had a partial specific volume of 0.73 cm3/g suggesting that the protein binds < 0.1 g of Triton/g of protein. A MW for the intact enzyme in the presence of 1% (wt/vol) Triton X-100 of 550,000 suggested that the enzyme may be a tetramer.This publication has 11 references indexed in Scilit:
- Solubilization, partial purification and properties of N-methylglutamate dehydrogenase from Pseudomonas aminovoransBiochemical Journal, 1977
- Characterization of membrane proteins in detergent solutionsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1976
- The size and detergent binding of membrane proteins.Journal of Biological Chemistry, 1975
- Pyruvate Carboxylase from Bacillus stearothermophilus: Molecular Size, Biotin Content and Subunit ConstitutionBiochemical Society Transactions, 1975
- [7] Analytical polyacrylamide gel electrophoresis and molecular weight determinationPublished by Elsevier ,1974
- Hydrophobic Chromatography: Use for Purification of Glycogen SynthetaseProceedings of the National Academy of Sciences, 1973
- Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergentsJournal of Supramolecular Structure, 1973
- Estimation of molecular size and molecular weights of biological compounds by gel filtration.1970
- Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide GelsNature, 1962
- A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein MixturesJournal of Biological Chemistry, 1961