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Enrichment of proteins with amino acid residues, employing p, p'-difluoro-m, m'-dinitrodiphenyl sulfone,

dc.contributor.authorBrazil, H.en_US
dc.contributor.authorSri Ram, J.en_US
dc.date.accessioned2006-04-13T14:43:13Z
dc.date.available2006-04-13T14:43:13Z
dc.date.issued1965-04en_US
dc.identifier.citationBrazil, H., Sri Ram, J. (1965/04)."Enrichment of proteins with amino acid residues, employing p, p'-difluoro-m, m'-dinitrodiphenyl sulfone,." Archives of Biochemistry and Biophysics 110(1): 205-209. <http://hdl.handle.net/2027.42/32033>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DVNJ59-11/2/aa869777f56e296b75278adb4617daecen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32033
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=14321855&dopt=citationen_US
dc.description.abstractThe bifunctional reagent, p, p'-difluoro-m,m'-dinitrodiphenyl sulfone, was employed to conjugate a variety of amino acids to the protein, gelatin. Among the amino acids tried, tyrosine conjugated most readily. The tyrosyl derivative of gelatin was characterized by electrophoretic, ultracentrifugal, and spectral studies. The conjugation of tyrosine to gelatin appeared to take place through the phenolic groups, although it was also shown to occur through the amino groups when the phenolic groups were blocked.en_US
dc.format.extent789356 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleEnrichment of proteins with amino acid residues, employing p, p'-difluoro-m, m'-dinitrodiphenyl sulfone,en_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USAen_US
dc.contributor.affiliationumDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USAen_US
dc.identifier.pmid14321855en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32033/1/0000076.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(65)90175-Xen_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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