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Free carboxylate groups required for transport of neutral amino acids by the Ehrlich ascites-tumor cell

dc.contributor.authorGarcia-Sancho, Javieren_US
dc.contributor.authorSanchez, Anaen_US
dc.contributor.authorChristensen, Halvor N.en_US
dc.date.accessioned2006-04-07T17:12:54Z
dc.date.available2006-04-07T17:12:54Z
dc.date.issued1977-03-01en_US
dc.identifier.citationGarcia-Sancho, Javier, Sanchez, Ana, Christensen, Halvor N. (1977/03/01)."Free carboxylate groups required for transport of neutral amino acids by the Ehrlich ascites-tumor cell." Biochimica et Biophysica Acta (BBA) - Biomembranes 465(2): 426-428. <http://hdl.handle.net/2027.42/22973>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T1T-47TGDHR-15F/2/66d7fff7115cdc3691f1aa415525df4den_US
dc.identifier.urihttps://hdl.handle.net/2027.42/22973
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=16250354&dopt=citationen_US
dc.description.abstractAlthough uncharged structures analogous to the carboxyl group of the amino acid molecule have served in place of that group for transport into some cells, we find that substitution either by the carboxamide group or by the chloromethyl ketone group eliminates inhibition of transport Systems A or L of the Ehrlich ascites tumor cell. Comparison of the loss of System L transport on acidification shows that the pH at which this loss occurs is correlated with pK'1 of the amino acid substrate, suggesting that transport is terminated by protonation of the site-bound carboxylate group.en_US
dc.format.extent147170 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleFree carboxylate groups required for transport of neutral amino acids by the Ehrlich ascites-tumor cellen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan, Ann Arbor, Mich. 48109, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan, Ann Arbor, Mich. 48109, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan, Ann Arbor, Mich. 48109, U.S.A.en_US
dc.identifier.pmid16250354en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/22973/1/0000540.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2736(77)90094-3en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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