Abstract
Isolated H+-ATPase from chromaffin granules was reconstituted into liposomes and the resultant proteoliposomes were further purified by Ficoll density gradient centrifugation. Studies by electron microscopy showed that proteoliposomes had particle structures (average diameter, about 10 nm) on their outer surface. These particles could be removed from the proteoliposomes by cold treatment. Immuno-electron microscopy showed that these particles were recognized by antibodies against the hydrophilic sector of the enzyme. These results indicate that the H+-ATPase has a peripheral membrane structure similar to that of F1-ATPase.
| Original language | English |
|---|---|
| Pages (from-to) | 92-96 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 291 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Oct 7 1991 |
Keywords
- Catalytic sector
- Chromaffin granule
- Extrinsic membrane sector
- F-like particle
- Vacuolar H-ATPase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Moriyama, Y., Yamamoto, A., Tashiro, Y., & Futai, M. (1991). Chromaffin granule H+-ATPase has F1-like structure. FEBS Letters, 291(1), 92-96. https://doi.org/10.1016/0014-5793(91)81111-K