Purification of component A of the soluble methane monooxygenase of Methylococcus capsulatus (Bath) by high-pressure gel permeation chromatography
- 1 June 1984
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 139 (2), 459-462
- https://doi.org/10.1016/0003-2697(84)90034-4
Abstract
No abstract availableThis publication has 6 references indexed in Scilit:
- Oxidation of Hydrocarbons by Methane Monooxygenases from a Variety of MicrobesPublished by Elsevier ,1980
- Characterization of the second prosthetic group of the flavoenzyme NADH–acceptor reductase (component C) of the methane mono-oxygenase from Methylococcus capsulatus (Bath)Biochemical Journal, 1979
- Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoproteinBiochemical Journal, 1978
- The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compoundsBiochemical Journal, 1977
- Ammonia oxidation by the methane oxidising bacterium Methylococcus capsulatus strain bathArchiv für Mikrobiologie, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970