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Differential binding of histidine-rich glycoprotein (HRG) to human IgG subclasses and IgG molecules containing kappa and lambda light chains

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dc.contributor.authorGorgani, Nicken_AU
dc.contributor.authorAltin, Josephen_AU
dc.contributor.authorParish, Christopheren_AU
dc.date.accessioned2015-12-13T23:25:00Z
dc.date.issued1999
dc.date.updated2015-12-12T09:23:03Z
dc.description.abstractIn previous studies we showed that the plasma protein histidine-rich glycoprotein (HRG) binds strongly to pooled human IgG. In the present work myeloma proteins consisting of different human IgG subclasses were examined for their ability to interact with
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/1885/92484
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc
dc.sourceJournal of Biological Chemistry
dc.subjectKeywords: immunoglobulin g; immunoglobulin light chain; antigen antibody complex; article; biosensor; controlled study; human; human cell; molecular weight; priority journal; protein binding; protein interaction; sequence homology; Humans; Immunoglobulin G; Immunog
dc.titleDifferential binding of histidine-rich glycoprotein (HRG) to human IgG subclasses and IgG molecules containing kappa and lambda light chains
dc.typeJournal article
local.bibliographicCitation.lastpage29640
local.bibliographicCitation.startpage29633
local.contributor.affiliationGorgani, Nick, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationParish, Christopher, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationAltin, Joseph, College of Medicine, Biology and Environment, ANU
local.contributor.authoruidGorgani, Nick, u950814
local.contributor.authoruidParish, Christopher, u6900322
local.contributor.authoruidAltin, Joseph, u4235798
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor110106 - Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
local.identifier.ariespublicationMigratedxPub23601
local.identifier.citationvolume274
local.identifier.doi10.1074/jbc.274.42.29633
local.identifier.scopusID2-s2.0-0033569757
local.type.statusPublished Version

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