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Cited by 284

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Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation

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Kagawa, Yasuo, Racker, Efraim·1966·Journal of Biological Chemistry

Abstract

Abstract 1. Evidence has been presented in this paper which greatly strengthens the suggestion that the spherical particles lining the inner membranes of mitochondria are the morphological representations of coupling factor 1 (ATPase). 2. With tritum-labeled ATPase it was shown that treatment of reconstituted particles with 2 m urea leads to a release of radioactivity which corresponded to the disappearance of the inner membrane spheres. 3. Certain salts, e.g. KI or KSCN were shown to facilitate the cold inactivation of ATPase in mitochondrial particles and to eliminate the inner membrane spheres. 4. Studies of the structural properties of reconstituted preparations of oligomycin-sensitive ATPase revealed characteristic fragments of membranes with inner membrane spheres. These preparations were essentially colorless and contained negligible amounts of respiratory enzymes. 5. A role of phospholipids in the organization of the membranous fragments was demonstrated.

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Metadata

Authors
Kagawa, Y., & Racker, E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1966-05
Volume
241
Issue
10
Pages
2475-2482
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1560885209
Cited by
284
References
0
FWCI
12.71
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation. https://app.cochat.ai/papers/10.1016/s0021-9258(18)96642-1
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Kagawa, Y., & Racker, E. (1966). Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)96642-1

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.