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)

Spleen cells from a CBF1 (BALB/c X C57BL/6) mouse immunized with rat tyrosine 3-monooxygenase were fused with NS-1 mouse myeloma cells. From 188 hybrid cells, 2 stable clones secreting anti-tyrosine 3-monooxygenase antibody were obtained. Antibody from one clone was coupled to CNBr-activated Sepharose 4B and the monoclonal antibody-Sepharose was shown to be very useful for isolating rat tyrosine 3-monooxygenase from crude preparations. Analyses by monoclonal antibody chromatography followed by SDS-polyacrylamide gel electrophoresis and by gel filtration revealed that tyrosine 3-monooxygenases from nerve cell bodies, nerve terminals, and adrenal medullae were indistinguishable with respect to their molecular structures. However, there were serious differences in the catalytic properties between the enzymes from the brain tissues and adrenal medullae, although there appeared to be no significant difference between the enzymes from nerve cell bodies and nerve terminals. The possibility that the activity of the enzyme may be strongly suppressed especially at the physiological pH in brain tissues is also discussed.
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PMID:A comparative study of tyrosine 3-monooxygenase from rat adrenal and brainstem. 258 40

Spleen lymphocytes from donor mice immunized against rabies virus were transferred into non immunised cyclophosphamide treated syngeneic mice. Antibody producing cells against rabies antigens were increased in the cyclosphosphamide treated recipient mice (p less than 0.01) as compared to then non treated recipient mice. A fusion was made with the splenic cells of cyclophosphamide treated recipient mice and SP2 murine myeloma cells 30 of 144 hypridoma plated welles were positive. There results suggest that cyclophosphamide immunosuppression inhibits the regulation of antibody production.
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PMID:[Increase of lymphocytes producing antibodies against rabies virus, using intrasplenic adoptive transfer in mice treated with cyclophosphamide]. 263 21

Balb/c mice were immunized with human plasmin-generated fibrinogen degradation product Y. Spleen cells were fused with P3X63-Ag8.653 myeloma cells. A clone (Y22) was found that produces monoclonal antibodies (MoAbs) with a strong reactivity with human fibrin and only a weak reactivity with fibrinogen in an enzyme immunoassay (EIA). Y22 also reacts with fibrin of rabbits, rats, sheep, and dogs. The antibodies are of the IgG1 kappa-type and appear to be directed against a conformation-dependent epitope in the D-domain of fibrin. Experiments with 99mTc-labeled Y22 in vitro show that Y22 binds rapidly to forming clots. 99mTc-Y22 also binds to preformed plasma clots in a plasma milieu, even in the presence of high concentrations of heparin. Clot localization experiments in rabbits and rats confirm the high fibrin specificity and the potential of 99mTc-Y22 for thrombus imaging in vivo.
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PMID:An antifibrin monoclonal antibody useful in immunoscintigraphic detection of thrombi. 266 52

Complementary DNA segments that encode different domains of human and rat androgen receptors were fused to the Escherichia coli trpE gene using pATH expression vectors. Fusion proteins expressed by the bacteria were used to immunize rats and rabbits to obtain polyclonal antibodies to androgen receptors. Spleen cells of immunized rats were fused with myeloma cells to obtain stable hybridomas that produced monoclonal antibodies. Gradient centrifugation and immuno-precipitation assays indicated that the antibodies interacted with androgen receptors specifically.
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PMID:Fusion proteins containing androgen receptor sequences and their use in the production of poly- and monoclonal anti-androgen receptor antibodies. 266 5

Two types of recombinant human IL-6 (rIL-6) were used for the development of specific monoclonal antibodies. The first was produced in E. coli and used for immunization, the second was produced in Chinese Hamster Ovary Cells (CHO) and used for screening. The complete translated sequence of the cDNA coding for human IL-6 was fused, in phase, to protein-A and the hybrid gene was fused to the strong lambda PR promoter. This protein was purified from bacterial extracts by chromatography on rabbit IgG-Sepharose columns. After six injections of the purified protein into mice, sera were tested for their binding titer in a solid phase radioimmunassay (sRIA) and for the specificity of binding by Western blots. In the sRIA, crude supernatants of CHO cells (harboring a plasmid containing the human IL-6 gene and expressing high levels of IL-6 but no protein-A or any bacterial antigen) were bound to a solid support, reacted with supernatants of the hybridomas and finally detected with [125I]-goat anti-mouse antibodies. Spleen cells derived from a mouse showing the highest binding titer were fused to mouse myeloma cells. The hybridomas were screened by the sRIA and several positive clones were isolated and characterized. One of the clones was found to neutralize the hybridoma growth factor activity of the rIL-6 from both sources. The same clone was also used for Western blots and for affinity purification of both natural and recombinant IL-6 (E. coli and CHO).
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PMID:Monoclonal antibodies for affinity purification of IL-6/IFN- beta 2 and for neutralization of HGF activity. 268 Sep 1

Spleen cells from BALB/c mice immunized against Echinococcus multilocularis were fused with mouse myeloma cells (P3X6.5.3.) in the presence of polyethylene glycol (PEG 1000), and the hybridomas were obtained. Of the 85 hybridomas, 23 were found to produce antibodies. Of the 23 cell lines, 13 hybridomas which produced a high titer of antibodies were cultured for cloning the cells by the limiting dilution method. Then 5 monoclonal antibodies were obtained. The immunoglobulin class of the monoclonal antibodies were IgM in one, IgG in 4. IgG monoclonal antibodies were studied by the ABC immunostain method. The germinal layer, brood capsules and protoscolices were stained. Germinal layer was especially stained by 4 monoclonal antibodies. However sections of liver, kidney, spleen and other parasites; anisakis, ascariasis lumbricoides, entamoeba histolytica and schistosoma japonicum were not stained with those monoclonal antibodies.
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PMID:[Production and characterization of monoclonal antibodies to Echinococcus multilocularis]. 268 34

Spleen cells from adult unprimed outbred (Swiss) and inbred (BALB/c) mice, either normal (no) or athymic-nude (nu) as well as spleen cells from Swiss nude mice bearing two different human tumors (BUR and PINQ), were fused with the mouse non-secreting myeloma cell line P3X63 Ag8-653. The supernatants of immunoglobulin secreting hybrids, all containing IgM, were screened for antibody activity against macromolecular antigens (autologous: actin, tubulin, myosin, dsDNA) and haptens (TNP, NP, NIP and NBrP). Furthermore, their idiotypic determinants were analyzed using a rabbit anti-idiotype which recognizes a major cross-reactive idiotype (IdD23) of BALB/c natural polyreactive autoantibodies. In all the mice studied, we identified: (1) hybrids reacting strongly with one or more haptens (10.7 to 37.8%) and (2) hybrids secreting natural monoclonal autoantibodies (NMoAb) with broad reactivities (polyreactive and/or oligoreactive) against autoantigens and/or haptens (11.4 to 26.8%). The results indicate that: (1) cells secreting natural autoantibodies with broad reactivities exist in both normal and nude mice, independently of the genetic background (inbred/outbred) of the mouse. However, in nude mice, the natural autoantibodies exhibit a more restricted pattern of reactivity (oligoreactive) compared to those of normal mice, and do not express the common idiotype IdD23 of natural polyreactive autoantibodies. (2) Tumors grafted into nude mice seem to induce the expression of polyreactive autoantibodies bearing the IdD23.
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PMID:Natural autoantibodies in nude and normal outbred (Swiss) and inbred (BALB/c) mice. 276 99

Spleen cells derived from rats naturally-infected with Mycoplasma pulmonis were stimulated in vitro, and then fused with a mouse myeloma cell line. The resulting hybridomas were screened for mycoplasma-specific Mabs by ELISA and for hemolysis-blocking activities. Fusions performed with in vitro-treated spleen cells yielded larger numbers of growth-positive wells and antibody secreting cells than untreated spleen cells from the same animals. Hybridomas derived from naturally-infected animals gave a higher percentage of hemolysin-specific monoclonal antibodies than did hyperimmunized animals. This indicated that B cell priming during mucosal infections can produce antigen-primed spleen cells. Stimulation of these cells in vitro can result in monoclonal antibodies against antigens not normally recognized during immunization with in vitro grown pathogenic bacteria.
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PMID:In vitro stimulation of nonimmunized, naturally infected rat spleen cells for the production of Mycoplasma pulmonis-specific monoclonal antibodies. 280 12

Spleen cells from BALB/c mice immunized with human leukocyte interferon gamma (HuIFN-gamma) were fused with mouse NSO myeloma cells. Nine hybridoma lines were found secreting monoclonal antibodies (MoAb) which were able to neutralize the antiviral activity of HuIFN-gamma. All nine MoAb inhibited also the antiproliferative activity of HuIFN-gamma. The ability of tested MoAb to inhibit both the antiviral and antiproliferative activities of HuIFN-gamma supports the suggestion that a common domain on HuIFN-gamma molecule might be responsible for both biological activities. However, ELISA and/or RIA proved unsuitable for detection of these specific MoAb.
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PMID:Monoclonal antibodies neutralizing the antiviral and the antiproliferative activities of human interferon gamma. 290 38

Spleen cells from mice immunised with group-A type-M15 streptococci and boosted with purified IgG Fc-receptor (FcR) from this type were fused with Sp 2/0 mouse myeloma cells. The resulting hybridomas were screened by ELISA for antibody production. Two IgM-secreting cell lines were selected. The monoclonal antibodies and ascites fluids inhibited the binding of 125I-labelled human IgG and IgG Fc-fragments to group-A type-M15 streptococci. The monoclonal antibodies also displaced purified FcR towards the anode in electrophoresis. They opsonised group-A type M-15 streptococci for phagocytosis by human granulocytes in the presence of fresh human serum. It was concluded that FcR is important for group-A streptococcal virulence.
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PMID:Monoclonal opsonic mouse antibodies specific for streptococcal IgG Fc-receptor. 294 29


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