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)

Immunization of BALB/c mice with natural purified HIV antigen, fusion of spleen cells with myeloma cells and subsequent selection of hybrid clones using recombinant gag antigen of HIV gave hybridomas producing monoclonal antibodies (MCA) to HIV. The immune blotting method demonstrated that 3 clones interacted with protein p24 and 4 clones with protein p17 of HIV. Competitive EIA led to a conclusion that the resulting MCA detected at least 3 antigenic determinants in proteins, products of gag gene of HIV. The potentials of using these MCA for the detection of viral antigen in HIV-infected continuous cell lines were demonstrated.
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PMID:[The properties of monoclonal antibodies to HIV gag gene proteins]. 179 79

BALB/c mice were immunized with gelonin, a 30 kD glycoprotein (type 1 RIP) from the seeds of Gelonium multiflorum. By polyethylene glycol-induced fusion of isolated spleen cells with the myeloma cell line NS-1, three different hybridomas were obtained. Two of them were found to secrete antibodies of the IgG1 subclass, whereas the third cell line produced antibodies of the IgM type. The IgG1-secreting cell lines were adapted to serum-free medium conditions, and the antibodies were isolated from the culture supernatant. The isolated antibodies recognize independent epitopes on the gelonin molecule. The toxicity of gelonin in reticulocyte lysates was not affected when the protein was incubated with the antibodies. The IgG1s exhibit average affinity constants of about 10(9) M-1 and 10(10) M-1, respectively, as determined by a solid-phase EIA using the avidin-biotin system.
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PMID:Monoclonal antibodies to gelonin: production and characterization. 203 35

The immunization procedure and immunogen characteristics required to optimize the production of anti-steroid monoclonal antibodies have been studied. Five different estradiol-bovine serum albumin conjugates were tested for immunizing mice, as were two different immunization protocols (high and low dose) and the effect of varying the myeloma/spleen cell ratio for cell fusion. Antibody-producing hybridomas, obtained using the spleens of 9 high anti-steroid titre mice, were detected by RIA and EIA. The latter method was less specific than the former for higher affinity anti-estrogen antibodies. All the immunogens elicited anti-estrogen antibodies and the efficiency appeared related to the steroid density on the immunogen rather than the chemical nature of the derivative or the immunization and fusion protocols. Thirty-six anti-estrogen producing hybridomas were detected. Comparison showed that all the immunogens elicited antibodies in a wide range of affinities and specificities. None of the antibodies recognized corticosteroids or progesterone. Cross reactions with testosterone and other estrogens were not clearly related to the nature of the immunogen except that estradiol coupled to the BSA via its carbon 17 yielded antibodies specific for steroids with a non-derivatized phenolic A-ring.
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PMID:Comparison of monoclonal antibodies to estradiol obtained from structurally different immunogens. 225 85

Two hybridoma cell lines producing monoclonal antibodies (MAbs) to mycoplasmas were established by fusion of mouse myeloma and spleen cells obtained from mice immunized with whole cell Mycoplasma pneumoniae antigens. The MAbs designated as MYC-4 and MYC-9 bound to a single M. pneumoniae protein band with approximate molecular weights of 150,000. In dot-EIA both MAbs reacted with ten Mycoplasma spp., two serovars of Ureaplasma urealyticum and Acholeplasma laidlawii. The MAbs have great potential to be used as an antibody probe for the rapid screening of cell cultures and hybridomas for mycoplasmal contamination.
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PMID:Development and application of monoclonal antibodies for the detection of cell infecting mycoplasmas. 251 56

The transcription factor PEA1 (a homologue of AP1 and c-jun) is highly active in several fibroblast cell lines, compared to its low activity in a myeloma and an embryo-carcinoma (EC) cell line. Serum components are essential to attain these high levels of PEA1 activity in fibroblasts. This serum requirement is abrogated by transformation with the oncogenes c-Ha-ras, v-src and polyoma middle T (Py-MT) but not by immortalization with polyoma large T (Py-LT), v-myc, c-myc or SV40 large T (SV40T). Expression in myeloma cells of the same transforming oncogenes, as well as v-mos and c-fos, activates PEA1, whereas expression of the same immortalizing oncogenes and EIA does not. These results suggest that a common target for transforming oncogenes is PEA1. Serum components have no effect on PEA1 activity in the myeloma and EC cell lines. In contrast, retinoic acid treatment of F9 EC cells augments PEA1 activity. These results suggest that transforming oncogene expression compensates for the absence of cell type-specific factors which are required to activate PEA1. Activation of PEA1 may lead to altered transcription of a set of transformation-related genes.
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PMID:Transforming but not immortalizing oncogenes activate the transcription factor PEA1. 314 63

A double antibody sandwich immunoassay (EIA) was developed for the detection of Salmonella. The assay utilizes a beta-galactosidase-murine myeloma monoclonal antibody (M467) conjugate prepared with the heterobifunctional coupling reagent, N-succinimidyl 3-(2-pyridyldithio) propionate (SPDP) and uses 4-methyl umbelliferyl beta-D-galactoside as a fluorogenic substrate for the enzyme. The EIA is sensitive and rapid, and compared favorably with the conventional cultural technique in the analysis of 60 feed samples naturally contaminated with Salmonella. Proteins or natural contaminants from the sample did not interfere in the assay.
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PMID:A fluorescent enzyme immunoassay for Salmonella detection. 328 71

Spleen cells from Balb C mice immunized with purified Yu human myeloma IgE were fused with NS-1 mouse myeloma cells. After initial EIA screening for antibody-secreting cells, 20 hybrids were further characterized for cell growth, ascites production, antibody titer, specificity and affinity. Immunoglobulins purified from ascites fluid obtained from selected clones were labelled with beta-galactosidase. Combinations were made using either antibodies as capture and as conjugate against calibrated human IgE plasma samples. The combination of monoclonal anti IgE X b 10-22 as a capture antibody and X b 6-16 as a conjugate gave the best sensitivity and slope in EIA. It was successfully used in a sensitive two-step-enzyme-immunoassay for total IgE. The X b 6-16 conjugate was also assayed for the detection of allergen specific IgE antibodies. The results presented and discussed indicate that monoclonal antibodies could favourably substitute for polyclonal anti IgE antibodies in such assays.
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PMID:Monoclonal antibodies to human IgE: utilization for total IgE quantification and estimation of allergen specific IgE antibodies. 639 32

A new system for the screening of hybrid cultures in high number for possible production/secretion of antibodies (immunoglobulin) is presented. In the hybridoma technique for the production of monoclonal antibodies, myeloma cells are fused with B-lymphoblasts. This fusion is induced and often polyethylene glycol is used for this. Soon after fusion, a multitude of small colonies appears. Because of the biochemical characteristics of the myeloma cells, a selection, which only leaves fused cells, is possible. Among these colonies of fused cells, some will be antibody producing and secreting, and some of these will have the correct specificity. This specificity is towards the antigen originally used for immunization of the animal (often mouse). Because of the high number of fused cells, it is important to eliminate competition among different clones, wherefore seeding is done in microtest plates. Even so, more fused cells can end up in the same well, and competition can occur. Therefore, it is important to identify the clones secreting antibody of correct specificity as soon as possible. In the systems employed until now, medium had to be removed from the culture microtest plates. This induces a change in composition with replenishment, and so is not desired too often. Furthermore, this pipetting of small amounts of medium is laborious having 5, 10, or more plates. Therefore, a new system has been developed, which does not remove any medium, that has EIA sensitivity, is fast, and with very few necessary pipettings. The system uses a transferred solid phase, and is called NUNC-TSP-Screening System.
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PMID:Early screening for hybrid antibodies. 667 30

Two hybridomas producing monoclonal antibodies (MAbs) were prepared by fusing myeloma cells (Sp2/0-Ag14) with mouse spleen cells immunized with purified spirosin from Yersinia enterocolitica SYT-11-72 (YE72). The antibodies produced by them were designated MAbs-S5 and S27. They were IgG2a and IgG1, respectively, both with kappa light chains. MAbs-S5 and S27 reacted specifically with spirosin from YE72. On Western blotting after limited proteolysis with Staphylococcus aureus V8 protease, YE72 spirosin revealed peptide fragments of 35 and 37 kDa reacting markedly with MAb-S5, which suggested the presence of an antigenic determinant on these fragments. By cellular fractionation of YE72 and subsequent EIA and Western blot analysis, spirosome was shown to be present in the cytoplasm of YE72.
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PMID:Monoclonal antibodies to spirosin of Yersinia enterocolitica and analysis of the localization of spirosome by use of them. 752 8

Six hybridoma cell lines (AP1-AP6) secreting monoclonal antibodies (McAb) against PAI-1 were obtained by fusing the murine myeloma cell line SP2/0 with the spleen cells from Balb/c mouse immunized with recombinant PAI-1 expressed in E. coli. These antibodies were purified by SPA affinity chromatography. All McAbs recognized rPAI-1 and PAI-1 from the human hepatoma cell line HepG2. The titers of ascites were more than 10(6). The antibody-antigen affinity constants (Kaff) for anti-PAI-1 McAb measured by EIA were between 3.45 x 10(7)-1.05 x 10(10) M. AP2 and AP3 McAbs were effective in quenching the activity of PAI-1. Partial quenching of PAI-1 activity was achieved with AP4, AP5 and AP6 McAbs respectively. AP1 McAb had no effect upon PAI-1 activity. Three of the six McAbs (AP1, AP4 and AP5) bound to the PAI-1/t-PA complex, while the others did not. The PAI-1 was purified 51 folds to homogeneity from serum free medium of HepG2 with the recovery rate of 92% by one-step procedure using Sepharose 4B conjugated with anti-PAI-1 McAb (AP1, AP3 and AP4). A sandwich ELISA for the measurement of PAI-1 antigen in human plasma was developed, based on anti-PAI-1 McAb against non-overlapping epitopes. The mean value of plasma PAI-1 for the healthy donors was 24.7 +/- 7.75 ng/ml measured by ELISA.
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PMID:Preparation, characterization and application of monoclonal antibodies against PAI-1. 780 88


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