A soluble form of cytochrome b_5, with a 413/280 nm ratio of nearly unity, has been isolated and purified from porcine kidney using fractional precipitation, ion exchange resins, and gel filtration procedures. The cytochrome b_5 shows heat stability up to 50° and is stable in the pH range 6.0 to 8.5. The oxidized protein exhibits an absorption maximum at 413 nm, while the reduced form shows three peaks: 423, 526, 556 nm. Molecular weight determinations have given variable results, suggesting the possibility of a polymer composed of four and eight units of a 13,500 molecular weight protomer. This study has used no lipases, proteases, or detergents in the solubilization of the cytochrome, and the possibility exists that the cytochrome found represents newly formed cytochrome b_5 which is as yet unattached to the microsomes, and which reflects the form found in intact cells.
| Identifer | oai:union.ndltd.org:BGMYU2/oai:scholarsarchive.byu.edu:etd-9290 |
| Date | 01 April 1973 |
| Creators | Klingler, M. Dean |
| Publisher | BYU ScholarsArchive |
| Source Sets | Brigham Young University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses and Dissertations |
| Rights | http://lib.byu.edu/about/copyright/ |
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