Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Six hybridomas that produce monoclonal antibodies to different antigenic determinants of heterogeneous pig IgG and of pig anti-Dnp antibodies were obtained by fusion between spleen cells from BALB/c mice immunized with non-specific pig IgG and the myeloma line P3-X63-Ag8.653. Antigenic determinants which correspond to individual monoclonal antibodies were located in the individual domains of the IgG molecule by investigating the interaction of monoclonal antibodies with Fab, Fc, and pFc' fragments and with kappa, lambda, and gamma polypeptide chains. To evaluate the interaction, a quantitative equilibrium competitive radioimmunoassay was developed and [14C]formaldehyde-labelled non-specific pig IgG served as labelled antigen. Antibodies PGG-01, PGG-04, and PGG-06 were shown to be directed against determinants in the C lambda domain, antibody PGG-03 very probably against the determinant in the C chi domain, and antibodies PGG-02 and PGG-05 against determinants in the CH3 domain. Antibodies PGG-02 and PGG-05 are highly selective for IgG subpopulations; when combined, they interact with no more than 42% of the heterogeneous IgG population. These two antibodies can be used as a basis for preparing a complete set of reagents for identification of individual subclasses.
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PMID:Limited enzymatic cleavage of pig immunoglobulin and of specific antibodies. V. Monoclonal antibodies to individual fragments and polypeptide chains. 243 58

To obtain antibodies against the individual chains of the T cell receptor (TCR) complex, we have produced chimeric proteins containing domains from immunoglobulin (Ig) and TCR polypeptide chains. Basically, the Ig light chains were used as carriers for the TCR constant (C) region domains. The exons which encode the main body of the C regions of the alpha, beta and the related gamma polypeptide chains were "engineered" into the intronic region between the rearranged Ig variable (V) region and C kappa region genes. All three chimeric genes were expressed in myeloma cells, and the proteins of expected apparent molecular weight were produced. Secreted proteins containing the C beta domain were purified from the culture supernatant by using anti-kappa antibody affinity columns, and two rabbits were then immunized with the purified protein. Both rabbits produced antibodies able to immunoprecipitate the heterodimeric TCR protein.
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PMID:A novel approach for preparing anti-T cell receptor constant region antibodies. 308 59

Streptococcal group A polysaccharide-specific antibodies were raised by the method of somatic cell hybridization. Spleen cells of experimentally unprimed BALB/c and C57BL/6 mice were activated in vitro by the streptococcal vaccine and fused with the Sp2/0-Ag14 line at times o, 35, 70, and 105 h thereafter. Hybridomas were obtained at all times independent of the addition of thymocyte-conditioned medium. Occurrence of specific hybridomas for the T cell-dependent A-CHO, however, required activation for greater than 35 h. Low responder C57BL/6 splenocytes fused at considerably higher fusion efficiency to yield specific hybridomas than high responder spleen cells 105 h after activation by antigen. The isotypes of A-CHO-specific antibodies comprised predominantly mu and kappa polypeptides; however, gamma 3, alpha, and gamma polypeptide chains were also identified. All specific antibodies were agglutinating the group A streptococcal cells; this agglutination was fully inhibited by the addition of 1% N-acetyl-D-glucosamine, the immune determinant sugar of the A-CHO. Three hybridomas obtained by fusion of BALB/c splenocytes 105 h after activation were cloned and grown as tumours in the peritoneal cavity of BALB/c mice. The monoclonal antibodies in the ascites did not precipitate the A-CHO but continued to agglutinate group A streptococcal cells in a hapten inhibitable fashion with different specificity profiles. Antibody from clone 21S36.1 was coprecipitable upon addition of A-CHO with a gamma G3 monoclonal hybridoma-derived antibody in a ratio of 1/7 while the other two monoclonal gamma M antibodies and the S117 myeloma protein were not. The result suggests that antibody 21S36.1 recognizes one chain terminal determinant of the A-CHO.
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PMID:Antistreptococcal group A antibodies: production after in vitro activation and hybridization of mouse spleen cells. 702 May 69