Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production

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dc.contributor.authorStrachan A.F.
dc.contributor.authorShephard E.G.
dc.contributor.authorBellstedt D.U.
dc.contributor.authorCoetzee G.A.
dc.contributor.authorVan Der Westhuyzen D.R.
dc.contributor.authorDe Beer F.C.
dc.date.accessioned2011-05-15T16:03:24Z
dc.date.available2011-05-15T16:03:24Z
dc.date.issued1989
dc.description.abstractHuman serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (>90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at >7 M-urea. By immunizing with apo-SAA adsorbed to acid treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.
dc.description.versionArticle
dc.identifier.citationBiochemical Journal
dc.identifier.citation263
dc.identifier.citation2
dc.identifier.issn2646021
dc.identifier.urihttp://hdl.handle.net/10019.1/12605
dc.subjectamyloid a protein
dc.subjectisoprotein
dc.subjecturea
dc.subjectamyloid a protein blood level
dc.subjecthuman
dc.subjectpriority journal
dc.subjectprotein structure
dc.subjectAdsorption
dc.subjectAmyloid Protein SAA
dc.subjectAntibodies
dc.subjectAntigens
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectHuman
dc.subjectHydrogen-Ion Concentration
dc.subjectImmunization
dc.subjectIsoelectric Point
dc.subjectLipoproteins, HDL
dc.subjectProtein Conformation
dc.subjectSalmonella
dc.subjectSolubility
dc.subjectSolutions
dc.subjectSupport, Non-U.S. Gov't
dc.subjectUrea
dc.subjectWater
dc.titleHuman serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production
dc.typeArticle
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