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Article: Purification of duck immunoglobulins: An evaluation of protein A and protein G affinity chromatography

TitlePurification of duck immunoglobulins: An evaluation of protein A and protein G affinity chromatography
Authors
Issue Date1995
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/vetimm
Citation
Veterinary Immunology And Immunopathology, 1995, v. 44 n. 2, p. 169-180 How to Cite?
AbstractDuck serum proteins binding to protein A Sepharose CL-4B and protein G Sepharose 4 Fast Flow and eluted at pH 2.8 or 11.5 were characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis, radial/immunodiffusion against defined anti-immunoglobulin (Ig) reagents, and by the reactivity in immunoelectrophoresis of antisera raised in rabbits inoculated with the eluates. The results indicated that IgY (previous nomenclature 7.8S IgG) and IgY (ΔFc) (previously 5.75 IgG) bound to protein A efficiently and to protein G weakly, while IgM bound to protein A and protein G weakly. Some binding of non-Ig proteins also occurred. Attempts to separate the non-Ig proteins from the Igs by elution at different pHs (5.0, 4.0, 3.0 and 2.5) were unsuccessful, but it was found that precipitation of Igs in day-old duck serum with Na 2SO 4, followed by chromatography on protein A Sepharose, yielded relatively pure IgY. The efficient binding of the duck IgYs to protein A resembles high affinity binding of mammalian Igs but cannot be attributed to the Fc, as it is in mammals, since the IgY (ΔFc) does not have an Fc region. Instead, binding probably occurs through unique histidine residues occurring predominantly in the CH I domain.
Persistent Identifierhttp://hdl.handle.net/10722/173209
ISSN
2015 Impact Factor: 1.664
2015 SCImago Journal Rankings: 0.864
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorHiggins, DAen_US
dc.contributor.authorCromie, RLen_US
dc.contributor.authorLiu, SSen_US
dc.contributor.authorMagor, KEen_US
dc.contributor.authorWarr, GWen_US
dc.date.accessioned2012-10-30T06:28:32Z-
dc.date.available2012-10-30T06:28:32Z-
dc.date.issued1995en_US
dc.identifier.citationVeterinary Immunology And Immunopathology, 1995, v. 44 n. 2, p. 169-180en_US
dc.identifier.issn0165-2427en_US
dc.identifier.urihttp://hdl.handle.net/10722/173209-
dc.description.abstractDuck serum proteins binding to protein A Sepharose CL-4B and protein G Sepharose 4 Fast Flow and eluted at pH 2.8 or 11.5 were characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis, radial/immunodiffusion against defined anti-immunoglobulin (Ig) reagents, and by the reactivity in immunoelectrophoresis of antisera raised in rabbits inoculated with the eluates. The results indicated that IgY (previous nomenclature 7.8S IgG) and IgY (ΔFc) (previously 5.75 IgG) bound to protein A efficiently and to protein G weakly, while IgM bound to protein A and protein G weakly. Some binding of non-Ig proteins also occurred. Attempts to separate the non-Ig proteins from the Igs by elution at different pHs (5.0, 4.0, 3.0 and 2.5) were unsuccessful, but it was found that precipitation of Igs in day-old duck serum with Na 2SO 4, followed by chromatography on protein A Sepharose, yielded relatively pure IgY. The efficient binding of the duck IgYs to protein A resembles high affinity binding of mammalian Igs but cannot be attributed to the Fc, as it is in mammals, since the IgY (ΔFc) does not have an Fc region. Instead, binding probably occurs through unique histidine residues occurring predominantly in the CH I domain.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/vetimmen_US
dc.relation.ispartofVeterinary Immunology and Immunopathologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshChickensen_US
dc.subject.meshChromatography, Affinity - Veterinaryen_US
dc.subject.meshDucks - Immunologyen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshEvaluation Studies As Topicen_US
dc.subject.meshFemaleen_US
dc.subject.meshImmunodiffusion - Veterinaryen_US
dc.subject.meshImmunoglobulins - Isolation & Purificationen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNerve Tissue Proteinsen_US
dc.subject.meshRabbitsen_US
dc.subject.meshStaphylococcal Protein Aen_US
dc.titlePurification of duck immunoglobulins: An evaluation of protein A and protein G affinity chromatographyen_US
dc.typeArticleen_US
dc.identifier.emailLiu, SS:stephasl@hku.hken_US
dc.identifier.authorityLiu, SS=rp00372en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0165-2427(93)05300-4en_US
dc.identifier.pmid7747399-
dc.identifier.scopuseid_2-s2.0-0028861843en_US
dc.identifier.volume44en_US
dc.identifier.issue2en_US
dc.identifier.spage169en_US
dc.identifier.epage180en_US
dc.identifier.isiWOS:A1995QF50800006-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridHiggins, DA=7202960434en_US
dc.identifier.scopusauthoridCromie, RL=6602318233en_US
dc.identifier.scopusauthoridLiu, SS=37102450400en_US
dc.identifier.scopusauthoridMagor, KE=6602171467en_US
dc.identifier.scopusauthoridWarr, GW=7102489206en_US

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