Chromaffin granule H+-ATPase has F1-like structure

Yoshinori Moriyama; Akitsugu Yamamoto; Yutaka Tashiro; Masamitsu Futai

doi:10.1016/0014-5793(91)81111-K

Chromaffin granule H⁺-ATPase has F₁-like structure

Yoshinori Moriyama, Akitsugu Yamamoto, Yutaka Tashiro, Masamitsu Futai

Faculty of Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

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	https://doi.org/10.1016/0014-5793(91)81111-K
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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10.1016/0014-5793(91)81111-K

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title = "Chromaffin granule H+-ATPase has F1-like structure",

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.",

keywords = "Catalytic sector, Chromaffin granule, Extrinsic membrane sector, F-like particle, Vacuolar H-ATPase",

author = "Yoshinori Moriyama and Akitsugu Yamamoto and Yutaka Tashiro and Masamitsu Futai",

note = "Funding Information: a grant for a Research Program on {\textquoteleft}Creation of New Materials through Intelligent Design{\textquoteright} from ISIR, Osaka University, and a Human Frontier ScienceP rogram ResearchG rant.",

year = "1991",

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doi = "10.1016/0014-5793(91)81111-K",

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AU - Moriyama, Yoshinori

AU - Yamamoto, Akitsugu

AU - Tashiro, Yutaka

AU - Futai, Masamitsu

N1 - Funding Information: a grant for a Research Program on ‘Creation of New Materials through Intelligent Design’ from ISIR, Osaka University, and a Human Frontier ScienceP rogram ResearchG rant.

PY - 1991/10/7

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AB - 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.

KW - Catalytic sector

KW - Chromaffin granule

KW - Extrinsic membrane sector

KW - F-like particle

KW - Vacuolar H-ATPase

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