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

Masahiro Kasahara | Zendy; Peter C. Hinkle | Zendy

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

Author(s) -

Masahiro Kasahara,

Peter C. Hinkle

Publication year - 1976

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.73.2.396

Subject(s) - liposome , sonication , diafiltration , chemistry , cytochalasin b , solubilization , biochemistry , chromatography , fraction (chemistry) , microsome , ultrafiltration (renal) , membrane , biophysics , in vitro , biology , microfiltration

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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