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A solid support for affinity chromatography that covalently binds thiol groups via a cleavable connector arm

dc.contributor.authorSingh, Pratapen_US
dc.contributor.authorLewis, Sidney D.en_US
dc.contributor.authorShafer, Jules A.en_US
dc.date.accessioned2006-04-07T17:22:09Z
dc.date.available2006-04-07T17:22:09Z
dc.date.issued1980-09en_US
dc.identifier.citationSingh, Pratap, Lewis, Sidney D., Shafer, Jules A. (1980/09)."A solid support for affinity chromatography that covalently binds thiol groups via a cleavable connector arm." Archives of Biochemistry and Biophysics 203(2): 774-779. <http://hdl.handle.net/2027.42/23162>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DN491V-1YB/2/af947328c32dbdcab857580e72a22d2ben_US
dc.identifier.urihttps://hdl.handle.net/2027.42/23162
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7458353&dopt=citationen_US
dc.description.abstractPreparation of an agarose derivative (MPE-agarose) containing a maleimido group which is attached to agarose via a cleavable phenyl ester linkage is described. MPE-agarose was shown to react with the thiol groups in glutathione, bovine serum albumin, bovine hemoglobin, and yeast and rabbit muscle glyceraldehyde 3-phosphate dehydrogenase. Treatment of the resulting agarose-linked compounds for 10 min with 1 hydroxylamine (pH 7) resulted in the cleavage of the phenyl ester linkage, and release of the maleimido derivative of the compound from the gel. In the case of hemoglobin and glyceraldehyde 3-phosphate dehydrogenase noncovalent interactions between the gel and the released protein lowered the amount of protein which dissolved in the hydroxylamine solution upon cleavage of the phenyl ester linkages. Noncovalently absorbed protein could be removed from the gel, however, by washing the gel with 2 guanidine hydrochloride after treatment with hydroxylamine. Derivatives of MPE-agarose should prove useful in affinity chromatography and immunoabsorption where it is difficult to elute material bound to conventional affinity supports.en_US
dc.format.extent600333 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleA solid support for affinity chromatography that covalently binds thiol groups via a cleavable connector armen_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 Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.identifier.pmid7458353en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/23162/1/0000087.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(80)90238-6en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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