A study of some oxidative enzymes of baker's yeast |
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| Authors: | SMITH L |
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| Affiliation: | 1. Euclid Techlabs, LLC, 365 Remington Blvd, Bolingbrook, USA;2. Department of Condensed Matter Physics and Materials Science, Brookhaven National Laboratory, Upton, NY 11973, USA;3. Materials Science and Engineering Division, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA |
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| Abstract: | - 1.1. A method is described whereby cytochrome c oxidase, cytochrome c peroxidase, and catalase activities can be measured independently in suspensions of broken yeast cells.
- 2.2. The activity of the yeast peroxidase in the presence of added peroxide is about five times greater than that of cytochrome c oxidase in oxidizing reduced cytochrome c, while the concentration of catalase in yeast is very low compared to that of the two other enzymes.
- 3.3. The yeast extract contains a very active cytochrome c reductase which is linked to succinic dehydrogenase. The DPN-and TPN-linked dehydrogenase systems do not seem to be functioning in the yeast extract.
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