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dc.contributor.authorCarruthers, Anthony
dc.contributor.authorHelgerson, Amy L.
dc.contributor.authorHebert, Daniel N
dc.contributor.authorTefft, Robert E. Jr.
dc.contributor.authorNaderi, Shokofeh
dc.contributor.authorMelchior, Donald L.
dc.date2022-08-11T08:08:57.000
dc.date.accessioned2022-08-23T16:13:28Z
dc.date.available2022-08-23T16:13:28Z
dc.date.issued1989-12-01
dc.date.submitted2008-03-21
dc.identifier.citationAnn N Y Acad Sci. 1989;568:52-67. <a href="http://dx.doi.org/10.1111/j.1749-6632.1989.tb12490.x">Link to article on publisher's site</a>
dc.identifier.issn0077-8923 (Print)
dc.identifier.doi10.1111/j.1749-6632.1989.tb12490.x
dc.identifier.pmid2698078
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33630
dc.description.abstractHuman red cell sugar transport shows profound changes upon cellular aging.' As the human erythrocyte glucose transport protein shares more than 98% primary, structural homology with the rat and rabbit brain glucose transport can be isolated from human red cells in large (mg) quantities and, owing to the relative ease of manipulation of red cell contents by forming resealed ghosts, erythrocyte sugar transport may provide a useful experimental model for the study of the effects of the aging process on a protein-mediated membrane process. In this short paper we examine how the catalytic activity of the human erythrocyte glucose transport protein is modified by intracellular ATP and calcium, by extracellular calcium, and by the physical and compositional properties of its resident membrane bilayer.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2698078&dopt=Abstract ">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1111/j.1749-6632.1989.tb12490.x
dc.subjectAdenosine Triphosphate; Biological Transport; Calcium; *Carbohydrate Metabolism; Erythrocytes; Humans; Lipid Bilayers
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleEffects of calcium, ATP, and lipids on human erythrocyte sugar transport
dc.typeJournal Article
dc.source.journaltitleAnnals of the New York Academy of Sciences
dc.source.volume568
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/3
dc.identifier.contextkey467853
html.description.abstract<p>Human red cell sugar transport shows profound changes upon cellular aging.' As the human erythrocyte glucose transport protein shares more than 98% primary, structural homology with the rat and rabbit brain glucose transport can be isolated from human red cells in large (mg) quantities and, owing to the relative ease of manipulation of red cell contents by forming resealed ghosts, erythrocyte sugar transport may provide a useful experimental model for the study of the effects of the aging process on a protein-mediated membrane process. In this short paper we examine how the catalytic activity of the human erythrocyte glucose transport protein is modified by intracellular ATP and calcium, by extracellular calcium, and by the physical and compositional properties of its resident membrane bilayer.</p>
dc.identifier.submissionpathgsbs_sp/3
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages52-67
dc.contributor.studentDaniel N. Hebert


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