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PMID: 1061142 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 2 ·1976-02-00 ·Pages 396-400

Kasahara M, Hinkle PC

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.

MeSH Terms
Biological Transport/drug effects Carrier Proteins/blood,metabolism Cytochalasin B/pharmacology Depression, Chemical Erythrocytes/metabolism Ethanol/pharmacology Glucose/metabolism Kinetics Liposomes/metabolism Mercury/pharmacology Sonication
Chemicals
Carrier Proteins Liposomes Cytochalasin B Ethanol Mercury Glucose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kasahara M
Hinkle P C
References (31)
31 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.73.2.396
Published
1976-02-00
Pages
396-400
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC335915
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.73.2.396 PMC Full Text View journal details
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