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The role of protein carboxyl groups in carbohydrate-concanavalin a interaction

dc.contributor.authorHassing, Gordon S.en_US
dc.contributor.authorGoldstein, Irwin J.en_US
dc.contributor.authorMarini, M.en_US
dc.date.accessioned2006-04-17T16:24:34Z
dc.date.available2006-04-17T16:24:34Z
dc.date.issued1971-07-25en_US
dc.identifier.citationHassing, G. S., Goldstein, I. J., Marini, M. (1971/07/25)."The role of protein carboxyl groups in carbohydrate-concanavalin a interaction." Biochimica et Biophysica Acta (BBA) - Protein Structure 243(1): 90-97. <http://hdl.handle.net/2027.42/33604>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B73GJ-47S62TN-1B/2/428fda048dcdcc03d6031d56c8e1977ben_US
dc.identifier.urihttps://hdl.handle.net/2027.42/33604
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5121624&dopt=citationen_US
dc.description.abstract1. 1. The role of carboxyl groups in the binding of specific carbohydrates to concanavalin A, the phytohemagglutinin of the jack bean, has been studied using two techniques: (1) H+ titration in the presence and absence of methyl [alpha]--mannopyranoside, a specifically bound carbohydrate ligand and (2) chemical modification of the protein carboxyl groups employing glycine methyl ester and a water-soluble carbodiimide, in the presence and absence of the mannoside.2. 2. It is shown that protein carboxyl groups are masked when concanavalin A is titrated in the presence of the sugar hapten and that this sugar glycoside also protects protein carboxyl groups from modification with glycine methyl ester.en_US
dc.format.extent460409 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleThe role of protein carboxyl groups in carbohydrate-concanavalin a interactionen_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 Biochemistry, Northwestern University Medical School, Chicago, Ill. 60611, U.S.A.; Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biochemistry, Northwestern University Medical School, Chicago, Ill. 60611, U.S.A.; Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biochemistry, Northwestern University Medical School, Chicago, Ill. 60611, U.S.A.; Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A.en_US
dc.identifier.pmid5121624en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/33604/1/0000108.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2795(71)90040-7en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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