Abstract

Receptors for C3b (C3R) in human spleen and kidney were studied using haemadsorption to cryostat sections. The indicator cells, ovine erythrocytes (E) coated with rabbit IgM antibody (A) and human C3b (EAC) adhered strongly to the glomeruli in renal tissue and to the white pulp of spleen. Titration experiments showed that avidity of the two populations of C3R was equal. Activity was independent of Ca++ and Mg++. Periodic acid, formaldehyde, high salt concentrations and trypsin abolished, whereas neuraminidase enhanced the activity. Various temperatures and pHs affected the two populations of C3R similarly. The results obtained indicate that the C3R in spleen and kidney are similar.

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