Matches in SemOpenAlex for { <https://semopenalex.org/work/W4313308919> ?p ?o ?g. }
Showing items 1 to 51 of
51
with 100 items per page.
- W4313308919 endingPage "525" @default.
- W4313308919 startingPage "517" @default.
- W4313308919 abstract "Abstract Human immunoglobulin (IgG) coupled with bis-diazo-benzidine (BDB-IgG) is capable of causing a release reaction from platelets in a manner similar to heat-aggregated IgG or antigen-antibody complexes. Various organic solvents, e.g., ethanol and acetone, also produce platelet-stimulating complexes. All these aggregated immunoglobulins caused the fixation of complement (C), although not strictly in parallel to their ability to cause the platelet release reaction. Myeloma proteins from the subclasses IgG1, IgG2 and IgG3, but not IgG4 or IgA, bind C, while all IgG subclasses, including IgG4, stimulate platelets. IgG3 proteins cause a poor release reaction but bind C well. The release reaction induced by human BDB-IgG is inhibited by monomeric IgG but not by bovine IgG or albumin. Partially purified C1 and purified Clq also inhibit the release reaction. The presence of Ca2+ is not required for any of these effects. It is concluded that for an aggregated immunoglobulin to stimulate platelets it is not necessary that it activate the complement enzymes in the classical way, but that either it may interact with a cell-bound Clq-like receptor, or the immunoglobulin possesses distinct, but closely situated, sites for platelet and C activation." @default.
- W4313308919 created "2023-01-06" @default.
- W4313308919 creator A5047763508 @default.
- W4313308919 creator A5064182826 @default.
- W4313308919 date "1972-09-01" @default.
- W4313308919 modified "2023-09-26" @default.
- W4313308919 title "The Effects of Aggregated Immunoglobulins on Human Blood Platelets in Relation to Their Complement-Fixing Abilities" @default.
- W4313308919 doi "https://doi.org/10.4049/jimmunol.109.3.517" @default.
- W4313308919 hasPublicationYear "1972" @default.
- W4313308919 type Work @default.
- W4313308919 citedByCount "27" @default.
- W4313308919 crossrefType "journal-article" @default.
- W4313308919 hasAuthorship W4313308919A5047763508 @default.
- W4313308919 hasAuthorship W4313308919A5064182826 @default.
- W4313308919 hasBestOaLocation W43133089191 @default.
- W4313308919 hasConcept C159654299 @default.
- W4313308919 hasConcept C185592680 @default.
- W4313308919 hasConcept C203014093 @default.
- W4313308919 hasConcept C2780267503 @default.
- W4313308919 hasConcept C2780898057 @default.
- W4313308919 hasConcept C55493867 @default.
- W4313308919 hasConcept C86803240 @default.
- W4313308919 hasConcept C89560881 @default.
- W4313308919 hasConceptScore W4313308919C159654299 @default.
- W4313308919 hasConceptScore W4313308919C185592680 @default.
- W4313308919 hasConceptScore W4313308919C203014093 @default.
- W4313308919 hasConceptScore W4313308919C2780267503 @default.
- W4313308919 hasConceptScore W4313308919C2780898057 @default.
- W4313308919 hasConceptScore W4313308919C55493867 @default.
- W4313308919 hasConceptScore W4313308919C86803240 @default.
- W4313308919 hasConceptScore W4313308919C89560881 @default.
- W4313308919 hasIssue "3" @default.
- W4313308919 hasLocation W43133089191 @default.
- W4313308919 hasOpenAccess W4313308919 @default.
- W4313308919 hasPrimaryLocation W43133089191 @default.
- W4313308919 hasRelatedWork W1977422126 @default.
- W4313308919 hasRelatedWork W2005154809 @default.
- W4313308919 hasRelatedWork W2010949326 @default.
- W4313308919 hasRelatedWork W2013166001 @default.
- W4313308919 hasRelatedWork W2108472544 @default.
- W4313308919 hasRelatedWork W2379042160 @default.
- W4313308919 hasRelatedWork W2390270540 @default.
- W4313308919 hasRelatedWork W2396153894 @default.
- W4313308919 hasRelatedWork W2418470149 @default.
- W4313308919 hasRelatedWork W2953256015 @default.
- W4313308919 hasVolume "109" @default.
- W4313308919 isParatext "false" @default.
- W4313308919 isRetracted "false" @default.
- W4313308919 workType "article" @default.