Studies of the oligomycin-sensitive ATPase from yeast mitochondria. Reconstitution of ATP-32Pi exchange in the presence of phospholipids
✍ Scribed by Ryrie, Ivan J.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 298 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0091-7419
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✦ Synopsis
Abstract
A purified preparation of the oligomycin‐sensitive ATPase from yeast mitochondria has been shown to elicit an oligomycin‐ and uncoupler‐sensitive ATP‐^32^P~i~ exchange in the presence of phospholipids. Reconstitution was normally achieved by dialysis of an ATPase‐phospholipid‐cholate mixture. Following this procedure, vesicles with diameters between 200 and 1,500 Å were seen by electron microscopy. As in mitochondria, ATPase activity in the reconstituted system was stimulated by a range of uncouplers which inhibited ATP‐^32^P~i~ exchange. These and other findings suggest that the coupling mechanism may still be intact within the ATPase complex.