Comparison of the homogeneous, primary anti-dextran B1355 antibody raised in BALB/c mice with protein 104E.

The primary antibody response to dextran B1355 in BALB/c mice is largely a homogenous IgM antibody. This antibody appears to be similar if not identical to the myeloma protein, protein 104E, for the following reasons: a) isoelectric focusing of the 7S monomers, separately and together in co-isoelectric focusing, give the same pattern, both in the presence and absence of 4M urea; b) the inhibition of lysis of the dextran-coated SRBC by specifically purified anti-dextran antibody and by protein 104E required essentially the same concentration of dextran B1355. This similarity was further demonstrated by plaque assays with dextran-coated SRBC, in which the formation of plaques was inhibited by free dextran. Inhibition of plaques produced by both types of cells required essentially the same concentration of dextran B1355. On these bases, there appears to be no difference in properties (or in structure) between the myeloma protein and the induced antibody.