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Reconstitution of D-glucose transport catalyzed by a protein fraction from human erythrocytes in sonicated liposomes.

Open access
Kasahara, M, Hinkle, P C·1976·Proceedings of the National Academy of Sciences

Abstract

A protein fraction was obtained from human erythrocyte ghosts by solubilization with Triton X-100 or octylglucoside. Triton X-100 was removed from the protein by Bio-Beads SM-2 and octylglucoside, by diafiltration. The solubilized protein fraction catalyzed D-glucose uptake when reconstituted in sonicated liposomes. The uptake was time dependent and inhibited by mercuric ions or cytochalasin B. The results indicate that the uptake represents transport of the sugar into the liposomes rather than binding to the reconstituted liposomes.

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Metadata

Authors
Kasahara, M., & Hinkle, P. C.
Venue
Proceedings of the National Academy of Sciences
Published
1976-02
Volume
73
Issue
2
Pages
396-400
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2021150756
Cited by
169
References
0
FWCI
8.66
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Reconstitution of D-glucose transport catalyzed by a protein fraction from human erythrocytes in sonicated liposomes. https://app.cochat.ai/papers/10.1073/pnas.73.2.396
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Kasahara, M., & Hinkle, P. C. (1976). Reconstitution of D-glucose transport catalyzed by a protein fraction from human erythrocytes in sonicated liposomes. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.73.2.396

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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.