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)

By using an indirect enzyme-linked immunosorbent assay, four monoclonal antibodies were selected after fusion of mouse P3-NS1-Ag4-1 myeloma cells with spleen cells isolated from BALB/c mice that had been immunized with aflatoxin M1 (AFM1) conjugated to bovine serum albumin. Two of these antibodies were found to be specific for AFM1 and were designated AMW-1 and AMW-4. The specificities of AMW-1, which had higher affinity to AFM1, were determined by a competitive direct enzyme-linked immunosorbent assay with peroxidase-AFM1 as the marker. The relative cross-reactivity of each toxin (relative to AFM1) with AMW-1, as determined by the amount of aflatoxin necessary to cause 50% inhibition of enzyme activity, was 12, greater than 40, 12, and greater than 40 for B1, B2, G1, and G2, respectively.
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PMID:Production and characterization of monoclonal antibodies against aflatoxin M1. 644 Apr 84

The hybrids (the CANS lines) between inflammatory macrophages from C57BL/6N (B6) mice (H-2b) and BALB/c mouse (H-2d)-derived myeloma cell line NS1 in the early period after cell fusion showed no macrophage functions. However, most of the hybrids expressed these functions after prolonged cultivation accompanied with chromosome loss. In contrast, the hybrids initially displaying myeloma functions (kappa light chain production) lost this function when they exhibited macrophage functions. We studied the expression of cell-surface antigens in these hybrids and found that hybrids in the early period after cell fusion codominantly expressed both parental cell H-2 antigens (H-2Kb, H-2Kd, and H-2Dd) but not the H-2Db antigen. On the other hand, aged hybrids strongly expressed the H-2d antigen but lacked the H-2Kb antigen. Alternatively, these aged hybrids with macrophage functions expressed antigen(s) as detected with antiaged CANS-196 cell sera and asialo GM1 antigen, both of which were thought to be found exclusively on macrophages. Thus, the expression of cell-surface antigens in these hybrids was greatly altered after cell fusion.
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PMID:Time course study of H-2 and other antigen expression by hybrids of a myeloma cell line with inflammatory macrophages. 646 88

In order to get more standardized reagents for blood group typing and to get more information on the chemical nature of blood group antigens we have immunized Balb/c mice with whole red blood cells and with sialoglycoprotein fraction from group OMMss cells. As fusion partners mouse myeloma cell lines P3-NS1/1-Ag 4-1 and X63-Ag8.653 were used. Several monoclonal antibodies were obtained, which showed specificity for the M/N antigens. Because of the relationship between M and N antigens this system is a very good example for studying the influence of different parameters on the reactivity of monoclonal antibodies. Each monoclonal antibody behaves like an individuum and for each antibody the dependence of the agglutination reaction of temperature, pH, buffer for dilution and medium, in which the reaction takes place, has to be investigated. Otherwise the results are not comparable and unspecific reactions might occur. By standardizing these parameters specific reactions were obtained and the antibodies might be used as routine reagents.
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PMID:Reactivity of monoclonal antibodies directed against blood group antigens M and N. 652 51

Hybrid cell lines have been derived from a fusion between mouse myeloma cell line, NS1/Ag 4-1, and spleen cells from BALB/c mice immunized with freshly resected osteosarcoma cells from an untreated patient. Of the 276 hybrids obtained, five secreted antibodies which bound to osteosarcoma tissues but not to autologous skin fibroblasts. Antibodies secreted by individual hybrids were tested for their reaction with a panel of human normal and tumor tissues in an immunofluorescence assay, and they displayed different specificities. Two of these antibodies, OST2 and OST4, bound to osteosarcoma tissues and to some other tumors and normal tissues. The antibodies from three of these five hybrids, OST6, OST7, and OST15, reacted with all of seven osteosarcoma tissues and one chondrosarcoma tissue but not with other malignant or benign tumors. Tests of various normal tissues were negative, except for weak binding to a subpopulation of chondrocytes in calcified areas of cartilage near the subchondral bone. Interestingly, none of the antibodies showed reactivity with three osteosarcoma cell lines, Te 85, Te 418, and MG 63. The experiments established the usefulness of the hybridoma technique in preparing monospecific antibodies against human osteosarcoma associated antigens. In particular, this study demonstrates that the use of freshly resected tumor tissues in preparing monoclonal antibodies would provide a necessary tool for the study of tumor associated antigens.
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PMID:[Detection of human osteosarcoma-associated antigens by monoclonal antibodies]. 657 22

Type IV collagen is one of the main constituents of basement membranes, yet it is unknown whether the structural framework at different sites is assembled from one unique type of molecule or whether different type IV collagen molecules exist. To study the composition, chemical identity, and organization of this protein in different organs we have prepared monoclonal antibodies to a type IV collagen preparation from human placenta. Swiss Webster mice were hyperimmunized, and splenic cells were fused with the three different myeloma cell lines SP2/0, NS1, and U1. Type IV collagen-specific hybrids were selected and cloned by limiting dilution and on hard agar. Monoclonal antibodies secreted by two clones were extensively characterized by ELISA-inhibition assay, immunoprecipitation, rotary shadowing, and immunofluorescence techniques. Unlike conventionally raised antibodies in rabbits, both monoclonal antibody reagents show species-specific binding exclusively to native type IV collagen from human placenta but not to a similar preparation from calf lung or to other types of collagen. After heat denaturation of the antigen binding was no longer observed. The M3F7 antibody-binding site is located within the triple helical domain of the type IV molecule, approximately 900 A removed from the amino terminal end as visualized by a metal shadow casting technique. The monoclonal antibody M3F7 precipitates material from pepsin-derived and radiolabeled type IV collagen, and analysis of the polypeptide chains in the immunoprecipitate by sodium dodecyl sulfate polyacrylamide gel electrophoresis suggests that two major fragments are contained in the precipitate, which yield polypeptides of about 100 and 50 kilodaltons. After rotary shadowing of antigen-antibody mixtures native collagen fragments of two different size classes that bind antibody are visualized. One fragment is approximately 1500 A in length, and the other measures about 2700 to 3000 A. The localization of the antigenic site on these fragments suggests that both are generated by pepsin cleavage at a site about 900 A removed from the amino terminal end. In immunofluorescence experiments the monoclonal antibodies stained all basement membranes in kidney, lung, placenta, or skin, suggesting that at least the type IV collagen molecule recognized by these monoclonal antibodies is shared by a variety of vascular and epithelial basement membranes.
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PMID:Methods in laboratory investigation. Monoclonal antibodies to type IV collagen: probes for the study of structure and function of basement membranes. 668 65

Monoclonal antibodies to deoxycorticosterone were produced. Mice were immunised with deoxycorticosterone-3-mono-oxime-BSA conjugate and spleen cells were then hybridised with NS1/1Ag4-1 mouse myeloma cells using 1500 mol. wt polyethylene glycol. The hybrids were grown in RPMI 1640 medium containing HAT to facilitate selection of positive clones. The clones and subclones were screened by using deoxycorticosterone-3-mono-oxime-[125I]iodohistamine. Dextran-coated charcoal was used for separation of antibody bound and free fractions. Two independent clones producing antibody which specifically binds labelled deoxycorticosterone were obtained. Cells from the two best sub-clones were used to raise ascites fluid. Comparison of these antibodies with one of the best conventional antisera previously raised in rabbits showed that the affinity constants were almost comparable (0.49-1.4 X 10(10) l/mol). Cross-reactivity of monoclonal antibodies with cortisol, corticosterone, testosterone and pregnenolone was lower than for polyclonal antisera, but for progesterone the cross-reactivity was similar in both cases. The assay sensitivity obtained with ascites fluid was comparable to that of conventional antibody (2.5 pg/ml). The dilution of ascites fluid which produced 50% binding of the label was 1:4,000,000. These results confirm that it is possible to produce monoclonal antibodies to corticosteroids.
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PMID:Production of high affinity monoclonal antibodies to deoxycorticosterone. 670 56

Spleen cells from Balb/c mice given multiple injections of intact human erythrocytes (group O, NN) were fused with NS1 myeloma cells. Culture fluids from the resulting hybrid cells were screened for agglutinating antibody against a panel of erythrocytes. One cell line, 2/23, secreted an IgM antibody which reacted more strongly with NN than with MM cells. Neuraminidase or papain treatment of erythrocytes abolished agglutination whereas trypsin treatment did not. Reactions with U- erythrocytes of different MN phenotypes confirmed the anti-N specificity of monoclonal antibody 2/23. This is the first report of monoclonal anti-N stimulated by the immunization of mice with intact erythrocytes.
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PMID:An interesting monoclonal anti-N produced following immunization with human group O, NN erythrocytes. 672 62

Monoclonal antibodies (mc/anti-LSP) have been prepared by polyethylene glycol fusion of P3/NS1/Ag4-1 myeloma cells with spleen cells from Balb/c mice hyperimmunized with human liver-specific membrane lipoprotein (LSP). Ten hybridomas, cloned by limiting dilution, produced mc/anti-LSP reacting (by ELISA) with human LSP but not with normal human plasma proteins nor with a variety of other proteins likely to co-purify with LSP. Three of these ( A15 /7, A9/63 and B20 ), producing high-titre IgG1 mc/anti-LSP, were biosynthetically radiolabelled and used as index antibodies. By competitive inhibition of binding of the index antibodies to LSP in an immunoradiometric assay, the ten hybridoma products were classified into four distinct groups according to their specificities for different epitopes in LSP. None of the index antibodies reacted, on ELISA, with glutaraldehyde-fixed PLC/PRF/5, Chang, Daudi or HSB-2 cell lines nor with human peripheral blood leucocytes. However, A15 /27 (but not A9/63 or B20 ) reacted with saponin-permeabilized PLC/PRF/5 and Chang cells and also with rabbit LSP. The results emphasize the polyantigenic nature of LSP and indicate that at least one of the mc/anti-LSP ( A15 /27) recognises a species cross-reactive antigen that is present in liver-derived cell lines.
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PMID:Production and preliminary characterization of monoclonal antibodies to human liver-specific lipoprotein (LSP). 672 82

By spleen cell fusion with NS1 myeloma, a mouse hybridoma was obtained which secretes an antibody directed against human renin. This monoclonal antibody recognizes human and monkey renin, but neither hog nor mouse. Preliminary experiments demonstrate the potential of this antibody for renin immunopurification and characterization.
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PMID:Monoclonal antibody against human renin. 678 95

Hybridomas were produced by fusing the NS1 mouse myeloma line, which does not produce mouse heavy chain Ig, with human peripheral B lymphocytes from a normal individual. Two vigorously growing colonies from this fusion were found to secrete human Ig heavy chains and were recloned. Two secondary clones, which secreted human chains, were again recloned. Among the tertiary clones, two were identified which produced intracellular human Ig chains, but did not secrete immunoglobulin. These tertiary clones were recloned, generating 6 quaternary clones which failed to produce human Ig heavy chains, and 15 quaternary clones which produced intracellular Ig chains. Hybrid clones from each successive subcloning were examined for their human chromosomal content and only those clones which were found to be individually chromosomally distinct, a total of 56 clones in all, were used to analyze the segregation of human chromosomes and human Ig heavy chain synthesis. Results of this study indicate concordant segregation of human Ig heavy chain synthesis and chromosome 14. These studies therefore confirm the previous assignment by C. M. Croce et al. (Proc. Natl. Acad. Sci. USA 1979. 76: 3416) of the genes for human Ig heavy chains to chromosome 14.
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PMID:Confirmation of the assignment of genes of human immunoglobulin heavy chains to chromosome 14 by analysis of Ig synthesis by man-mouse hybridomas. 679 25


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