Guinea pig 7S immunoglobulins (gamma(1) and gamma(2)) consist of two groups of molecules (K and L) bearing different types of L chains (kappa and lambda). Approximately one-third of the molecules in normal guinea pig gamma(2)-globulin bear the lambda- type of L chains, and all or most of the others bear kappa-chains. kappa- and lambda-chains have similar molecular weights.

Animals↗

PubMed1966

Quantitative variations in L chain types in guinea pig antihapten antibodies.

In guinea pig purified antihapten antibodies, the proportion of molecules bearing the kappa- or lambda-type of L chains (K or L molecules) may diverge markedly from that found in normal gamma(2)-globulins. This has been evaluated by precipitation of I(131)-labeled antibody preparations using a specific anti-lambda-chain antiserum. Anti-DNP antibodies isolated 3 wk after immunization of guinea pigs with DNP(65)-BGG antibodies, contain less than 1% of L molecules, while in pipsyl antibodies, isolated from the sera of animals immunized with pipsyl-BGG, the proportion of L molecules is significantly greater than in normal gamma(2)-globulins. Anti-DNP antibodies produced against conjugates of this hapten with carriers other than BGG (BSA, OVA, or poly-L-lysine) or with BGG with a small number of DNP groups (DNP(10)-BGG) contained a greater proportion of lambda-chain bearing molecules than anti-DNP antibodies isolated from late sera of guinea pigs immunized with highly conjugated DNP(65)-BGG. An increased percentage of L molecules was detected in preparations of anti-DNP(65)-BGG antibodies isolated early (10 days), when compared to those isolated later during the course of immunization. However, the level of L molecules in all these anti-DNP antibody preparations was always considerably below that present in normal gamma(2)-globulin. The relative amounts of L molecules in distinct immunoglobulin families (gamma(1) and gamma(2)) in antibody preparations isolated from individual animals was remarkably similar.

Animals↗

PubMed1966

Antibody types in experimental animals and their biologic properties.

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Anaphylaxis↗

PubMed1966

The behavior of hapten-poly-L-lysine conjugates as complete antigens in genetic responder and as haptens in nonresponder guinea pigs.

30 to 40% of Hartley strain guinea pigs have previously been demonstrated to possess a dominant autosomal gene which enables them to recognize the antigenicity of hapten-poly-L-lysine conjugates as expressed by the development of both antihapten antibodies and delayed hypersensitivity to the immunizing antigen. In the present study, it was shown that PLL alone was weakly antigenic in such genetic responder animals. Immunization with DNP-PLL electrostatically combined with foreign albumins elicits the production of anti-DNP antibodies in all Hartley strain guinea pigs, although the percentage of animals demonstrating a delayed response to DNP-PLL and therefore considered genetic responders remains 30 to 40%. Immunization with nonantigenic polyanions combined with DNP-PLL does not produce such an effect. Some degree of PLL specificity of purified anti-DNP antibodies produced by genetic nonresponder animals by immunization with DNP-PLL combined with foreign albumins was demonstrated by means of fluorescence quenching.

Animals↗

PubMed1966

Studies on the effect of the carrier molecule on antihapten antibody synthesis. I. Effect of carrier on the nature of the antibody synthesized.

1. Fluorescence quenching has been calibrated, by comparison with equilibrium dialysis, for measurement of antibody-hapten association constants with guinea pig antibody to the 2,4-dinitrophenyl (DNP) determinant. The maximum quenching with all sites occupied which gave best agreement with equilibrium dialysis was found to be 100%. 2. The carrier to which the DNP-hapten is coupled influences significantly the amount, class (gamma(1) or gamma(2)), and affinity of the antibody of DNP specificity made by individual guinea pigs. 3. The affinities of gamma(1)- and gamma(2)-antibodies from individual guinea pigs are generally very similar. 4. Precipitin curves with gamma(1)-antibodies show more marked inhibition of precipitation in antigen excess than do precipitin curves with the less charged gamma(2)-antibodies, indicating the importance of nonspecific forces in the precipitation reactions.

Aminocaproates↗

PubMed1966

Studies on the effect of the carrier molecule on antihapten antibody synthesis. II. Carrier specificity of anti-2,4-dinitrophenyl-poly-l-lysine antibodies.

Equilibrium measurements of interactions of anti-DNP antibodies, prepared using DNP-PLL and several DNP-proteins for immunization, with DNP(0.6)-PLL(240) and with the univalent hapten, epsilon-DNP-L-lysine, were made utilizing the technique of fluorescence quenching. Carrier specificity of anti-DNP-PLL antibodies was demonstrated by a higher average intrinsic association constant (K(0)) of anti-DNP-PLL antibodies with DNP(0.6)-PLL(240) than with epsilon-DNP-L-lysine. The free energy contribution of the PLL carrier to the interaction of intact anti-DNP-PLL antibodies with DNP(0.6)-PLL(240) was from -0.8 to -2.1 kcal/mole. On the other hand, intact anti-DNP-protein antibodies displayed a lower energy of interaction with DNP(0.6)-PLL(240) than with epsilon-DNP-L-lysine of up to +2.4 kcal/mole. Fab' fragments of both anti-DNP-PLL and anti-DNP-BGG antibodies have K(0)'s with epsilon-DNP-L-lysine identical to the K(0)'s of the intact anti-DNP antibodies from which they were prepared. However, K(0) of interaction of Fab' fragments with DNP(0.6)-PLL(240) (a large proportion of the conjugated PLL molecules in this preparation bear more than one DNP group) is considerably lower than that of the intact antibody. Thus a cooperative effect in the binding of bivalent antibody and bivalent (or greater) antigen exists and is of the order of -1.2 to -2.0 kcal/mole of IgG antibody. Although the direct contribution of the carrier to the interaction of Fab' fragment of anti-DNP-PLL and DNP(0.6)-PLL(240) is -0.4 kcal/mole, the energy of carrier specificity, based upon consideration of cooperative effects and of repulsion of anti-DNP-protein antibodies for portions of the DNP-PLL determinants, is of the order of -3 kcal/mole (approximately 30% of total binding energy).

Animals↗

PubMed1966

Properties of antibodies cytophilic for macrophages.

Cytophilic activity for macrophages was shown to be a property possessed by most, if not all, of the complement binding 7S gamma(2)-population of guinea pig antibodies. Cytophilic antibodies were also demonstrated in rabbit and mouse antisera to sheep red cells. While each species antibody best sensitized homologous macrophages, cross species sensitization was also observed. The binding site for macrophages resides on the Fc fragment, therefore, on the H chains, and is destroyed by pepsin hydrolysis or reduction and alkylation. The binding reaction is reversible with a high rate of dissociation at 37 degrees C. Cytophilic activity is not complement dependent, and was shown to be that property of opsonizing antibody which provides the receptors that permit the binding of the antibody to the macrophage cell membrane in preparation for phagocytosis.

Alkylation↗

PubMed1966