A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue.
Open Access
- 1 July 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (14), 7926-7929
- https://doi.org/10.1016/s0021-9258(18)34271-6
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Occurrence of selenocysteine in the selenium-dependent formate dehydrogenase of Methanococcus vannieliiArchives of Biochemistry and Biophysics, 1979
- Nicotinic acid hydroxylase fromClostridium barkeri:Selenium-dependent formation of active enzymeFEMS Microbiology Letters, 1979
- Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteineBiochemistry, 1978
- Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.Journal of Biological Chemistry, 1977
- Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety.Proceedings of the National Academy of Sciences, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- The use of Coomassie Brilliant Blue G250 perchloric acid solution for staining in electrophoresis and isoelectric focusing on polyacrylamide gelsAnalytical Biochemistry, 1975
- [7] An anaerobic laboratoryPublished by Elsevier ,1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964