Vincent C, Revillard J P
Mol Immunol. 1983 Aug;20(8):877-84. doi: 10.1016/0161-5890(83)90085-8.
Serum components with binding activity towards free human beta 2 microglobulin (beta 2m) were investigated in healthy adults. The binding activity increased after treatment of the serum components by dissociating buffers (acid pH, 2-8 M urea, 3 M NaSCN, 6 M guanidine hydrochloride). This activity resided in serum IgG as shown by the following evidence: (1) recovery in the 160 K region after AcA 44 filtration, (2) association with the IgG fraction after purification by DEAE chromatography and AcA 34 filtration, (3) after immunopurification on beta 2m-Sepharose immunosorbent, the labeled eluted fraction was shown to bind to beta 2m-Sepharose and to protein A or anti-IgG-Sepharose. Pepsin-digested F(ab')2 fragments from serum IgG were treated by 3 M urea, then passed on beta 2m-Sepharose immunosorbent in order to prepare specific anti-beta 2m F(ab')2. Those fragments retained all the beta 2m binding capacity of the IgG fraction. Saturation analysis studies showed estimated K values between 1.5 and 9.5 X 10(9) L/M, depending on the preparation it was concluded that normal human serum contains minute amounts of auto-antibodies of relatively high affinities, specific for beta 2m.
