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dc.contributor.authorLeitch, Jeffry M.
dc.contributor.authorCarruthers, Anthony
dc.date2022-08-11T08:08:01.000
dc.date.accessioned2022-08-23T15:39:15Z
dc.date.available2022-08-23T15:39:15Z
dc.date.issued2007-02-13
dc.date.submitted2009-02-18
dc.identifier.citationAm J Physiol Cell Physiol. 2007 Feb;292(2):C974-86. Epub 2006 Aug 23. <a href="http://dx.doi.org/10.1152/ajpcell.00335.2006">Link to article on publisher's site</a>
dc.identifier.doi10.1152/ajpcell.00335.2006
dc.identifier.pmid16928769
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26122
dc.description.abstractHuman erythrocyte glucose sugar transport was examined in resealed red cell ghosts under equilibrium exchange conditions ([sugar](intracellular) = [sugar](extracellular), where brackets indicate concentration). Exchange 3-O-methylglucose (3MG) import and export are monophasic in the absence of cytoplasmic ATP but are biphasic when ATP is present. Biphasic exchange is observed as the rapid filling of a large compartment (66% cell volume) followed by the slow filling of the remaining cytoplasmic space. Biphasic exchange at 20 mM 3MG eliminates the possibility that the rapid exchange phase represents ATP-dependent 3MG binding to the glucose transport protein (GLUT1; cellular [GLUT1] of
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16928769&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1152/ajpcell.00335.2006
dc.subject3-O-Methylglucose
dc.subjectAdenosine Triphosphate
dc.subjectBiological Transport
dc.subjectCell Size
dc.subjectCytoplasm
dc.subjectEquilibrative Nucleoside Transporter 1
dc.subjectErythrocyte Membrane
dc.subjectErythrocytes
dc.subjectGlucose
dc.subjectGlucose Transporter Type 1
dc.subjectHumans
dc.subjectMicroscopy, Electron, Scanning
dc.subjectModels, Biological
dc.subjectUridine
dc.subjectMembrane transport; erythrocytes; GLUT1
dc.subjectMedical Biochemistry
dc.subjectMedical Biophysics
dc.subjectPhysiological Processes
dc.titleATP-Dependent Sugar Transport Complexity in Human Erythrocytes
dc.typeJournal Article
dc.source.journaltitleAmerican journal of physiology. Cell physiology
dc.source.volume292
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/bmp_pp/61
dc.identifier.contextkey724049
html.description.abstract<p>Human erythrocyte glucose sugar transport was examined in resealed red cell ghosts under equilibrium exchange conditions ([sugar](intracellular) = [sugar](extracellular), where brackets indicate concentration). Exchange 3-O-methylglucose (3MG) import and export are monophasic in the absence of cytoplasmic ATP but are biphasic when ATP is present. Biphasic exchange is observed as the rapid filling of a large compartment (66% cell volume) followed by the slow filling of the remaining cytoplasmic space. Biphasic exchange at 20 mM 3MG eliminates the possibility that the rapid exchange phase represents ATP-dependent 3MG binding to the glucose transport protein (GLUT1; cellular [GLUT1] of </p>
dc.identifier.submissionpathbmp_pp/61
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pagesC974-C986


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