Abstract
Reviewing old protocols, it was found that Raji, a CR2-posistive cell line, binds both endogenous (e-C3) and exogenous C3 (i-C3). The processing of i-C3 to an i-C3b-like protein and their fixation to CR2 isoforms resulted in the formation of heterodimers whose units might be linked via thioester by low m.w. molecule(s). In an attempt to study the origin of the low m.w. molecules, it was found that they were detected following I(12)⁵-C3d treatment with NHS or hi-S. Indirect evidence would suggest that the products of C3 fragment fixation could have a short half-life and that the aromatic residues present in C3d might have different physico-chemical characteristics than those present in C3c. The surface hydrophobicity expressed by these aromatic residues could be required for the fixation of C3 or CR2 fragments to cell surface proteins.