rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1997-9-26
|
pubmed:abstractText |
The affinity of D-glucose and the transport inhibitor cytochalasin B (CB) for the glucose transporter Glut1 was studied at 5-42 degrees C by quantitative frontal affinity chromatography on sterically immobilized human red cell membrane vesicles, and on proteoliposomes containing reconstituted red cell membrane proteins. Glut1 in the vesicles showed the highest glucose affinity; the dissociation constant Kd(glc) was nearly constant (16 +/- 3 mM) from 15 degrees C to 37 degrees C. For Glut1 in proteoliposomes Kd(glc) decreased from 56 mM at 5 degrees C to 26 mM at 42 degrees C. The CB-Glut1 affinity was strongest around 20 degrees C and was mostly higher with the vesicles, Kd (CB) being 49 nM at 19 degrees C. The entropy and entropy and enthalpy changes for the interactions were calculated.
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0021-9673
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
776
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
87-91
|
pubmed:dateRevised |
2009-1-15
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pubmed:meshHeading |
pubmed-meshheading:9286081-Adult,
pubmed-meshheading:9286081-Chromatography, Affinity,
pubmed-meshheading:9286081-Erythrocyte Membrane,
pubmed-meshheading:9286081-Glucose,
pubmed-meshheading:9286081-Glucose Transporter Type 1,
pubmed-meshheading:9286081-Humans,
pubmed-meshheading:9286081-Hydrogen-Ion Concentration,
pubmed-meshheading:9286081-Ligands,
pubmed-meshheading:9286081-Lipid Bilayers,
pubmed-meshheading:9286081-Liposomes,
pubmed-meshheading:9286081-Membranes,
pubmed-meshheading:9286081-Monosaccharide Transport Proteins,
pubmed-meshheading:9286081-Temperature,
pubmed-meshheading:9286081-Thermodynamics
|
pubmed:year |
1997
|
pubmed:articleTitle |
Glucose affinity for the glucose transporter Glut1 in native or reconstituted lipid bilayers. Temperature-dependence study by biomembrane affinity chromatography.
|
pubmed:affiliation |
Department of Biochemistry, Uppsala University, Sweden.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|