Biomedical subjects

J V Wells

Publications and source records attributed to J V Wells.

At least 55 records · Page 3Linked to original sources

PubMed1973

Human anti-IgM iso-antibodies: detection of IgM allotypic markers.

IgG class antibodies against human IgM were detected in a human subject up to a titer of 1:1024 against 5 of a group of 23 monoclonal Waldenström macroglobulins. Inhibition studies confirmed at least one antigenic determinant shared by the 5 IgMs. The determinant was present on the mu chain but required tertiary structure for its full expression. Inhibition of the reaction between the antibodies to IgM and erythrocytes coated with 2 of the 5 IgMs was obtained at titers of 1:2 to 1:16 with 51.0% of 300 normal sera (85.2% of sera from 122 Caucasian, 26.1% of sera from 23 Negro, and 27.7% of sera from 155 Japanese individuals). This inhibition was independent of the serum IgM concentration. Family studies indicated that the determinant was inherited according to basic Mendelian laws and appears to be the first allotypic marker on human serum IgM. We have designated it Mm 1.

Antigen-Antibody Reactions↗

PubMed1973

Localization of idiotypic antigenic determinants in the Fv region of murine myeloma protein MOPC-315.

Rabbit antisera were prepared against the idiotypic determinants of the mouse IgA myeloma protein-315, its purified heavy and light chains, and the Fv fragment comprising the variable region of both heavy and light chains. Agar diffusion demonstrated a line of identity between protein-315 and its Fv fragment against either homologous antiserum. Protein-315 and Fv fragment were labeled with (125)I and reacted with their anti-idiotypic antisera. Inhibition studies confirmed that the Fv fragment contained all the idiotypic specificities present in the intact protein. Fv was as effective as protein-315 on a weight basis in inhibiting the reaction between anti-idiotypic antiserum and protein-315. Protein-315 has high affinity for the 2,4-dinitrophenyl group, and such ligands can inhibit the reaction between protein-315 and its anti-idiotypic antibodies. Hapten inhibition was also obtained with the Fv fragment and its anti-idiotypic antiserum, implying that Fv contains an intact combining site. In this system with protein-315 the antigenic determinants expressed as idiotypic specificities are entirely within the variable region and are not influenced in their expression by the constant region. We therefore suggest that, in general, idiotypic determinants are antigenic determinants of the Fv protions of immunoglobulins.

Aminobenzoates↗

PubMed1973