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Effect of sialidase on blood group specificity of hog submaxillary glycoproteins
dc.contributor.authorAminoff, Daviden_US
dc.contributor.authorMorrow, Marianne P.en_US
dc.date.accessioned2006-04-17T15:09:25Z
dc.date.available2006-04-17T15:09:25Z
dc.date.issued1970-07-03en_US
dc.identifier.citationAminoff, David, Morrow, Marianne P. (1970/07/03)."Effect of sialidase on blood group specificity of hog submaxillary glycoproteins." FEBS Letters 8(6): 353-358. <http://hdl.handle.net/2027.42/32733>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T36-447N04R-4Y/2/6494b87ff5eb45b12531a270cb235986en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32733
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11947612&dopt=citationen_US
dc.description.abstractHogs can be divided into three phenotypes A, H and In, depending on the ability of extracts of their submaxillary glands to inhibit the agglutination of human A cells with human anti-A, and human O cells with eel-anti-H serum. Evidence is here provided that the inactive glycoprotein, In, represents H active glycoprotein containing additional N-glycolyl neuraminic acid, which stereospecifically masks the H determinant, [alpha] (1 --&gt; 2)-L-fucosyl residue.en_US
dc.format.extent449844 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleEffect of sialidase on blood group specificity of hog submaxillary glycoproteinsen_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.affiliationumDepartments of Internal Medicine (Simpson Memorial Institute) and Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48104, U.S.A.en_US
dc.contributor.affiliationumDepartments of Internal Medicine (Simpson Memorial Institute) and Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48104, U.S.A.en_US
dc.identifier.pmid11947612en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32733/1/0000101.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0014-5793(90)80012-8en_US
dc.identifier.sourceFEBS Lettersen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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