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Properties of Catalase Purified from Whole Cells and Peroxisomes ofn-Alkane-GrownCandida tropicalis
| Content Provider | Scilit |
|---|---|
| Author | Yamada, Takao Tanaka, Atsuo Fukui, Saburo |
| Copyright Year | 1982 |
| Description | Journal: Journal of Biological Inorganic Chemistry Peroxisomes appear profusely, in harmony with a marked enhancement of catalase activity level, in yeast cells growing on n-alkanes or higher fatty acids as the sole carbon source. Catalase (H2O2:H2O2 oxidoreductase, EC 1.11.1.6) was purified to homogeneity from the crude extract and from the peroxisome-containing particulate fraction of alkane-grown Candida tropicalis cells. The purified enzyme from each source was a similar protein of molecular weight 210000 composed of four identical subunits of molecular weight 54000, namely a kind of homotetramer. The enzyme contained one molecule of heme per subunit, giving the absorption spectrum characteristic of hemoprotein. Beta-(3,4-Dihydroxyphenyl)-L-alanine served as a substrate for the peroxidatic reaction by the enzyme. Ouchterlony double-diffusion analysis and immunochemical titration with rabbit antiserum against peroxisomal catalase of n-alkane-grown C. tropicalis have indicated that cytoplasmic catalase of the yeast is immunologically indistinguishable with peroxisomal catalase. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1982.tb06712.x/pdf |
| Ending Page | 521 |
| Page Count | 5 |
| Starting Page | 517 |
| ISSN | 09498257 |
| e-ISSN | 14321327 |
| DOI | 10.1111/j.1432-1033.1982.tb06712.x |
| Journal | Journal of Biological Inorganic Chemistry |
| Issue Number | 3 |
| Volume Number | 125 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 1982-07-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Inorganic Chemistry Alkane Grown |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |
