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 interspecific hybridomas (heterohybridomas) secreting bovine monoclonal antibodies (MAbs) against respiratory syncytial (RS) virus were produced. Four of the heterohybridomas were formed using the mouse myeloma cell line NS1 as the fusion partner, one using NS0, and the remaining heterohybridoma was formed using a bovine X murine hybridoma as the fusion partner. Five heterohybridomas secreted bovine IgG1 and one secreted IgG2. All six MAbs recognized human subtype A and B viruses as well as bovine RS virus. They were specific for the fusion glycoprotein and reacted with a 140K dimer and a 70K monomer in a Western blot of native antigen; three also bound to the 46K F1 component and its 22K cleavage product in a blot of reduced antigen. Two of these MAbs neutralized RS virus infectivity, inhibited virus-induced fusion, lysed RS virus-infected cells in the presence of complement and protected mice against RS virus challenge.
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PMID:Production and characterization of bovine monoclonal antibodies to respiratory syncytial virus. 319 2

Hybridoma antibodies against bovine collagenase inhibitor were produced by fusion of myeloma cells NS-1 (P3-NS1-1) with spleen cells from mice hyperimmunized with collagenase inhibitor purified from the explant medium of bovine dental pulps. Hybridomas positive by an enzyme-linked immunosorbent assay (ELISA) for bovine collagenase inhibitor were cloned by the dilution method. Seventeen hybridomas producing antibodies were isolated, four of which also recognized purified human collagenase inhibitor in the ELISA. Using a monoclonal antibody-Sepharose affinity column, we easily purified both bovine and human collagenase inhibitors to homogeneity. They showed the same mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, corresponding to a molecular mass of 32,000 daltons.
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PMID:Monoclonal antibodies to bovine collagenase inhibitor. 331 76

Four cell lines producing monoclonal antibodies were obtained by fusion of NS1 myeloma cells with splenocytes of BALB/C mice immunized with only 1 microgram of each staphylococcal enterotoxin A, B, C1 and D by a modified technique of intrasplenic boosting. This procedure was considerably more efficient than the more commonly used intravenous boosting. The antibodies EC-A1, EC-B1, EC-C1 and EC-D1, all of the IgG1 subclass, have high affinities for the corresponding enterotoxins A, B, C1 and D, with dissociation constants of 1.4, 2.8, 1.4 and 1.5 nM respectively; in addition EC-B1 showed a high affinity (2.1 nM) for enterotoxin C1. All these antibodies recognize, by immunoblotting, the homologous purified enterotoxins as well as enterotoxins from the bacterial culture supernatants. A rapid indirect double sandwich ELISA using a pair of antibody preparations was developed, where monospecific monoclonal antibodies were used to coat plastic plates and polyspecific rabbit antibodies were used to detect the enterotoxins under field conditions. These antibodies which are capable of immunoadsorbing the enterotoxins from staphylococcal culture filtrates and from natural fluids such as milk, were used to immunopurify enterotoxins A, C1 and D. The homogeneity and integrity of the affinity purified toxins A, C1 and D was verified by direct automated Edman degradation and yielded single amino terminal sequences which were moderately homologous to those published previously for B and C1 enterotoxins.
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PMID:Production and characterization of monoclonal antibodies to staphylococcal enterotoxins: use in immunodetection and immunopurification. 332 90

The cell growth and monoclonal antibody production characteristics of two rat x mouse heterohybridoma cell lines, designated 187.1 and M1/9.3, were investigated using a biocompatible microencapsulation technology. Both cell lines, derived from the fusion of immunized rat spleen cells with either the NS1 or X63Ag8.653 myeloma cell lines, were found to reach a maximum intracapsular cell density of 1.3 to 1.5 X 10(7) cells/ml during a 27-d culture period. During this period, rat monoclonal antibody accumulated in the intracapsular space of both cultures to a final concentration of 2.0 to 2.8 mg/ml. Comparison of the concentration of rat monoclonal antibody in the extracapsular vs. the intracapsular space of both cultures indicated that significantly less than 1% of the antibody produced by the encapsulated hybridoma cells was capable of transiting the microcapsule membrane during the culture period. Due to the partition of the rat monoclonal antibody within the intracapsular space, the initial purity of the antibody harvested from 21-d microcapsule cultures of 187.1 and M1/9.3 cells was approximately 48 and 75% by weight, respectively. Analysis of the intracapsular protein by sodium dodecyl sulfoxide gel electrophoresis at different times during the culture period demonstrated that the principal contaminant associated with the unpurified antibody was bovine serum albumin.
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PMID:Production of rat monoclonal antibody from rat x mouse hybridoma cell lines using microencapsulation technology. 333 69

Monoclonal antibody specific for subgroup F enteric adenoviruses (EAds) was prepared by fusing P3-NS1/Ag4-1 mouse myeloma cells with lymphocytes from BALB/c mice immunized with G1105, an adenovirus type 41 (Ad41) strain. Monoclone 3F11/2H9, which specifically recognized Ad41, was successfully used as detector antibody in an enzyme-linked immunosorbent assay (ELISA). Additionally, previously prepared monoclones 5D8/2C2 and 2H6/1E11, recognizing Ad40 plus Ad41 and Ad40 alone, respectively, were used to study stool and/or tissue culture specimens from 106 patients with adenovirus-positive gastroenteritis. By ELISA, 91 had EAds (22 were Ad40 and 69 were Ad41) and 15 had non-EAds. ELISA results were in concordance with restriction endonuclease results for 38 of 39 specimens, with dot blot data for 19 of 20 specimens, and with neutralization test results for 74 of 78 specimens. ELISA was at least 10-fold more sensitive than direct electron microscopy was for the detection of EAds in stool specimens.
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PMID:Monoclonal antibody enzyme-linked immunosorbent assay for specific identification and typing of subgroup F adenoviruses. 334 24

BALB/c mice were immunized with uninduced K562 erythroleukemia cells and hybridomas were isolated after fusion of immune spleen cells to P3/NS1 murine myeloma cells. One selected hybrid, designated 10L-30, secreted an antibody of subclass immunoglobulin G2a which was specific for hematopoietic cells. Analysis of 10L-30 binding by complement-mediated cytotoxicity, indirect immunofluorescence, solid-phase radioimmunoassay, and mixed hemadsorption assay indicated that the 10L-30 antigen was expressed on the myeloid cell lines K562, KG-1A, KG-1, some B- and T-lymphoid cell lines, and all normal human peripheral blood T-lymphocyte samples tested, but was absent on the more differentiated myeloid cell lines HL-60, ML-2, ML-3, and normal blood granulocytes. Induction of erythroid differentiation in hemin-treated K562 cells caused a 10-fold reduction in 10L-30 binding. Human erythroid and granulocytic progenitor cells, platelets, erythrocytes, and reticulocytes were nonreactive, as were a variety of nonhematopoietic human tumor cell lines. Freshly isolated leukemic bone marrow samples from patients with M5 (2 of 5), M6 (2 of 2), acute lymphoid leukemia (9 of 14), and chronic myeloid leukemia in lymphoid blast crisis (1 of 1) were 10L-30 positive. The combined evidence indicates that the 10L-30 antigen is a normal, hematopoietic-specific differentiation antigen which is strongly expressed on both immature cells of the myeloid lineage and more generally in lymphoid ontogeny. The 10L-30 antigen may be a useful marker of both normal and leukemic hematopoietic differentiation.
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PMID:Distribution of a hematopoietic-specific differentiation antigen of K562 cells in the human myeloid and lymphoid cell lineages. 347 69

A series of hybridoma cell lines which produce monoclonal antibodies (MAbs) against recombinant human interleukin-2 (rIL-2) have been established by fusion of murine myeloma cell line P3-NS1-1-AG4-1 and spleen cells of BALB/c mice which had been immunized with rIL-2. 48 hybridoma strains were selected by a solid-phase screening method which produced MAbs reacting with IL-2: four MAbs, L-15, L-20, L-34, and L-61, exhibited strong inhibition of the proliferating effect of rIL-2 on IL-2-dependent cell lines, NK7 and CTLL-2. L-61, the most potent MAb among them, also neutralized natural human IL-2, while the other three MAbs were unreactive. All the four MAbs were specific to human IL-2: they did not cross-react with mouse or rat IL-2. These MAbs are expected to be useful tools in the investigation of IL-2 function.
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PMID:Neutralizing monoclonal antibodies against recombinant human interleukin-2. 349 4

A mouse-human hybridoma has been produced by fusing human splenocytes from a Cooley's anemia patient with the murine myeloma P3-NS1/1-Ag 4-1. The hybridoma is stable after 18 months and secretes human IgM. The antibody reacts with some H3N2 influenza A strains and detects an epitope that is part of the hemagglutinin antigen, but does not affect virus infectivity.
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PMID:A nonneutralizing human IgM monoclonal antibody inhibiting hemagglutination of H3N2 influenza A strains. 354 6

Four mouse myelomas commonly used for cell fusions (X63.Ag8.653, SP2/0, NS1, P3U1), 3 human myeloma-like cell lines (ARH77, U-266, GM1500) and 3 human x mouse hybridomas (SPAZ4, SA2, SA3) were compared for their heterokaryon formation and successful hybridoma growth after cell fusion with polyethylene glycol. The cells were stained with different fluorescent dyes which do not alter hybridoma growth or antibody secretion. After fusion myeloma cells containing at least 1 nucleus from a lymphocyte (heterokaryons) were counted from fluorescence photomicrographs and the heterokaryon frequency was calculated. Mouse myelomas fused at a frequency of 1-7%, whereas human myeloma lines showed a higher heterokaryon frequency ranging from 3-25%. In mouse fusions almost every well contained growing hybridomas showing a minimum hybridoma frequency of 2/10(6) lymphocytes. In human fusions the SPAZ4 and SA2 lines showed a heterokaryon frequency nearly as good as mouse myelomas, whereas U-266 yielded no growing hybridomas despite 20% heterokaryon frequency. Furthermore, human cell lines showed a high tendency of multikaryon formation whereas this phenomenon was rarely observed with murine and murine x human heterohybrids. In individual fusion experiments no correlation was found between heterokaryon formation and the number of growing hybridomas. Thus, our study shows that defects in hybridoma growth may not always result from lack of a successful fusion and human hybridomas might be more sensitive to post-fusion conditions.
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PMID:Estimation of heterokaryon formation and hybridoma growth in murine and human cell fusions. 362 81

Hybridomas were made between NS1/1-Ag4-1 mouse myeloma cells and peripheral blood lymphocytes from a sheep immunized with a testosterone-protein conjugate. ELISAs were developed to detect ovine IgG and specific ovine anti-testosterone and these were used to screen the colonies. Although the cells fused acceptably only 3% of colonies secreted detectable quantities of antibody. The antibody was secreted at low levels (2.5 ng/ml) but was of high affinity (KD = 7.63 x 10(-12) M/1). One line, O/M 4.22, continued to secrete in culture for four months until the termination of the experiment.
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PMID:Production of an ovine monoclonal antibody to testosterone by an interspecies fusion. 367 54


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