Analysis of immunoglobulins that bind to platelets from serum of XXXX with immune thrombocytopenia: molecular weight distribution.

@entity1 @entity3039 @entity1252
The nature of platelet- bindable immunoglobulins (PB-Ig) in serum has been investigated. PB-IgG, -A and -M were measured by an ELISA using platelets coated on microtitre plates. This assay detected alloantibodies at high serum dilutions. In 32 @entity1 with @entity1252 ( @entity1252 ) raised levels of at least one PB-Ig class were found in 18. To distinguish binding due to immune complexes, the molecular weight of PB-IgG was studied by gel filtration on Sepharose 4B. In sera from @entity1 with @entity3039 and @entity1252 , PB-IgG with Mr of primarily 150 Kd was observed, compatible with monomeric IgG antiplatelet antibodies. Levels of PB-IgG in serum were not related to total serum IgG. In sera from the @entity1 with @entity1252 and some with @entity3039 (most of whom had several of the features of @entity1252 ), PB-IgG with Mr of 200 Kd - greater than 1000 Kd was seen. In heat-aggregated preparations of normal IgG, PB-IgG with Mr up to 1000 Kd was also found. Rabbit IgG was able to block PB-IgG in fractions of high molecular weight in purified normal IgG, heat-aggregated normal IgG and in patient serum, but had no effect on the 150 Kd peak. In whole serum from @entity1 who had high molecular weight PB-IgG, the inhibitory effects of rabbit IgG were much less than in isolated high molecular weight column fractions. Thus although the majority of PB-IgG is monomeric antiplatelet antibody, some PB-IgG with higher molecular weight, characteristic of immune complexes, occurs in sera of some @entity1 with @entity3039 and it makes a small contribution to PB-IgG levels measured in whole serum.
