pubmed-article:1587638 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C0004358 | lld:lifeskim |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C0020852 | lld:lifeskim |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C1708096 | lld:lifeskim |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C0445604 | lld:lifeskim |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C1704711 | lld:lifeskim |
pubmed-article:1587638 | lifeskim:mentions | umls-concept:C0439098 | lld:lifeskim |
pubmed-article:1587638 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:1587638 | pubmed:dateCreated | 1992-6-23 | lld:pubmed |
pubmed-article:1587638 | pubmed:abstractText | Circulating IgG autoanti-IgE is detectable in a large proportion of individuals with allergic asthma where it is suggested to be potentially involved in the removal of IgE-allergen complexes. Since such a putative role will largely be determined by the subclass profile of complexed (i.e. IgE-bound) IgG anti-IgE, a study was undertaken to determine the subclass distribution of complexed IgG anti-IgE antibody in the sera of asthmatic patients. The study exploits the heat-labile property of IgE by heating (30 min at 56 degrees C) serum to liberate bound anti-IgE, pre- and post-heated sera are then assayed for IgG subclass anti-recombinant human Fc epsilon (rFc epsilon) activities by ELISA and any heat-induced increase in antibody activity is taken as a measure of complexed anti-IgE. This has revealed a disproportionately high amount of IgG4 in complexed (but not free) IgG anti-IgE. The propensity of IgG4 to form complexes with IgE has important biological consequences, particularly with regard to the activation of C1q and Fc gamma R by other subclasses. | lld:pubmed |
pubmed-article:1587638 | pubmed:language | eng | lld:pubmed |
pubmed-article:1587638 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1587638 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1587638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1587638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1587638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1587638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1587638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1587638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1587638 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1587638 | pubmed:issn | 1018-2438 | lld:pubmed |
pubmed-article:1587638 | pubmed:author | pubmed-author:ShakibFF | lld:pubmed |
pubmed-article:1587638 | pubmed:author | pubmed-author:MillsC SCS | lld:pubmed |
pubmed-article:1587638 | pubmed:author | pubmed-author:Powell-Richar... | lld:pubmed |
pubmed-article:1587638 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1587638 | pubmed:volume | 97 | lld:pubmed |
pubmed-article:1587638 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1587638 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1587638 | pubmed:pagination | 243-8 | lld:pubmed |
pubmed-article:1587638 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:meshHeading | pubmed-meshheading:1587638-... | lld:pubmed |
pubmed-article:1587638 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1587638 | pubmed:articleTitle | The recognition of a recombinant human Fc epsilon fragment by the subclasses of IgG autoanti-IgE: disproportional subclasses distribution of complexed autoantibody. | lld:pubmed |
pubmed-article:1587638 | pubmed:affiliation | Department of Immunology, University Hospital, Queen's Medical Centre, Nottingham, UK. | lld:pubmed |
pubmed-article:1587638 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1587638 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1587638 | lld:pubmed |