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Indications of spatial relations among structures recognizing amino acids and Na+ at a transport receptor site
dc.contributor.authorThomas, Edwin L.en_US
dc.contributor.authorChristensen, Halvor N.en_US
dc.date.accessioned2006-04-17T15:09:15Z
dc.date.available2006-04-17T15:09:15Z
dc.date.issued1970-07-27en_US
dc.identifier.citationThomas, E. L., Christensen, H. N. (1970/07/27)."Indications of spatial relations among structures recognizing amino acids and Na+ at a transport receptor site." Biochemical and Biophysical Research Communications 40(2): 277-283. <http://hdl.handle.net/2027.42/32729>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DX4HWP-84/2/5d87f2a724de80f861719983917f08e0en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32729
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5474782&dopt=citationen_US
dc.description.abstractThe orientation of the hydroxyl group on carbons 3 or 4 of proline, whether cis or trans, is decisive to the interaction between the amino acid and Na+ for a Na+-linked transport system of the pigeon erythrocyte and the rabbit reticulocyte. Consideration of this response in relation to other strong effects of the position of the hydroxyl group in two transport systems suggests that at the transport receptor site under study, the two substrates bind in juxtaposition, Na+ trans to the carboxyl group of the amino acid.en_US
dc.format.extent427172 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleIndications of spatial relations among structures recognizing amino acids and Na+ at a transport receptor siteen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48104, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48104, USAen_US
dc.identifier.pmid5474782en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32729/1/0000097.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(70)91006-5en_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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