| Autor: |
Oltmann, L. F., Reijnders, W. N. M., Stouthamer, A. H. |
| Zdroj: |
Archives of Microbiology; December 1976, Vol. 111 Issue: 1-2 p25-35, 11p |
| Abstrakt: |
Nitrate reductase A has been solubilized from purified cytoplasmic membranes by extraction with terl-amyl alcohol. The resulting aqueous solution contained monomeric reductase which polymerized slowly to dimers and tetramers with sedimentation coefficients of respectively 10.5, 16 and 23 Svedbergunits. The polymerization could be stopped to some extent by addition of a small amount of Triton X-100. These distinct entities of nitrate reductase A were separable on electro-focusing, DEAE-column chromatography and polyacrylamide gel electrophoresis, and have been proved to consist of similar subunits with molecular weights of 104000, 63000, and 56000 daltons. The molecular weights of monomeric nitrate reductase A was found to be about 240000 daltons. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
Full text from SpringerLink