Statements in which the resource exists as a subject.
PredicateObject
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
pubmed:journal
pubmed:citationSubset
IM
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
pubmed:meshHeading
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