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)

Antiidiotypic antibody (AIA) was raised in mice by immunization with MOPC 315 immunoglobulin A emulsified in Freund's adjuvant (FA). The antibody content of mouse serum was assessed by (a) its ability to inhibit rosetting of 2,4,6-trinitro-phenyl-sheep red blood cells around MOPC 315 myeloma cells, and (b) by a solid phase antigen-binding plate assay based on reactivity with 125I-Protein A and inhibition in the presence of dinitrophenyl aminocaproic acid. FA was necessary for the production of AIA to MOPC 315 immunoglobulin A. Some of the AIA-containing mouse sera were cytotoxic for MOPC 315 cells in the presence of guinea pig complement. However, cytotoxicity was not correlated with amount of AIA, as assessed by inhibition of rosette formation, nor was it specific for myeloma cells bearing the MOPC 315 idiotype. Furthermore, cytotoxicity could also be generated by immunization of mice with complete Freund's adjuvant, incomplete Freund's adjuvant, or the muramyl dipeptide portion of mycobacteria, all in the absence of MOPC 315 immunoglobulin A. Therefore, the complement-dependent cytotoxic antibodies in the AIA-containing antisera, which belonged to the immunoglobulin G and M classes, were likely directed against some component of FA. Myeloma cells which were not killed by anti-FA antiserum, as assessed by dye exclusion, were inhibited in their ability to secrete immunoglobulin and to form clones in agar.
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PMID:Induction of cytotoxic factors by immunization of mice with Freund's adjuvant components. 696 83

The specificity and kinetics of binding of purified monomeric human and murine myeloma immunoglobulins to Fc receptors were studied in a human promyelocytic cell line (HL-60). HL-60 cells contain approximately 20,000 Fc receptors per cell and bind human IgG1, IgG3 and mouse IgG2a with high affinity (dissociation constant of 5 to 10 nM). Kinetic studies of the binding of IgG1 to HL-60 cells demonstrate rapid exchange with ambient immunoglobulin with approximately one-half of the surface-bound IgG1 exchanging every 25 to 30 min at 37 degrees C. Estimation of the equilibrium binding constant from the rates of association and dissociation of IgG1 agrees well with the values obtained from Scatchard analysis of equilibrium binding of radioiodinated IgG1. Approximately one-half of the Fc receptors of HL-60 cells are capable of binding IgG1 complexed to Protein A. This result was independent of the concentration of Protein A (0.5 to 200 microM) or the time of incubation of IgG1 with Protein A. Studies in which Protein A was incubated with HL-60 cells at 37 degrees C then rapidly washed at 0 degrees C indicated that Protein A did not degrade Fc receptors or interact with the Fc receptor sites on HL-60 cells. The complexes formed between Protein A and IgG1 sedimented at 7 to 9S by ultracentrifugation. These results suggest that there are two types of Fc receptors on HL-60 cells, which can be distinguished by their ability to bind the IgG1-Protein A complex.
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PMID:Fc receptors of a human promyelocytic leukemic cell line: evidence for two types of receptors defined by binding of the staphylococcal protein A-IgG1 complex. 699 3

Monoclonal antibodies against 2 human lung carcinoma cell lines (E14 and BEN) were prepared by production and cloning of somatic cell hybrids between the murine myeloma NS1, and spleens from E14- and BEN-immune BALB/c mice. Approximately 2000 hybrid culture supernatants were screened for antibody simultaneously against the immunizing cell line and lung fibroblasts (573 Lu) using a radiolabelled Protein A binding assay. Although the vast majority secreted antibodies which recognized species-specific antigens, a few supernatants showed marked differential reactivity against E14 or BEN. These were cloned and subsequently tested against a panel of up to 25 human cell lines originating from different neoplastic and non-neoplastic tissues. Two anti-E14 clones (3E19.8 and 4EAB3.7) displayed preferential activity against lung cancer cell lines, but a low level of reactivity was also detectable with cell lines of different tissue provenance. The antibodies of 3 anti-BEN clones (7B3.5, 7B5.4, 7B17.7) likewise recognized antigens present to a higher density on lung cancer cell lines but were also reactive (to a variable extent for the different clones) with a diversity of other tumour cell lines. The antibodies of 2 further clones were exceptional in so far as one (7BC9.1) reacted only with BEN and WIDR (colorectal cancer) cells, while another (7B24.4) reacted, with apparent exclusivity, against BEN cells. With the exception of the latter, the distinction in antigen expression between many of the cell lines was quantitative rather than qualitative and the emergent picture is one of random expression of individual determinants on several disparate types of cancer cells, rather than restriction to cells of a given morphological type or histogenic derivation.
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PMID:Monoclonal antibodies against two human lung carcinoma cell lines. 717 57

Lymphocytes obtained from hilar and bronchial lymph nodes from 23 patients undergoing radical surgery for carcinoma of the bronchus were fused with established rat or mouse myeloma lines. 62% of the resultant hybrids were found to be secreting human Ig detected by a sensitive staphylococcal Protein A-coupled SRBC assay. Immunoglobulins synthesized by such hybrids were internally labelled with 3H-lysine and their antibody activity against a variety of membrane preparations determined. Nine monoclonal antibodies were found which bound to molecules on lung-cancer membranes and not on normal lung membranes from the same patient.
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PMID:Human monoclonal antibodies to lung-cancer antigens. 724 54

In this study we demonstrated that fetal calf serum (FCS) depleted of IgG by protein G affinity chromatography (G-FCS) is superior to whole FCS or serum-free culture media as a culture supplement for the production of purified IgG monoclonal antibodies (MAb). One hundred ml FCS was applied to a 25 ml protein G Sepharose 4 Fast Flow Column, which was shaken gently for 2 days at 4 degrees C. The procedure was repeated using a protein G column for an additional day. G-FCS was used at a concentration of 5% in RPMI 1640 medium to grow the mouse myeloma cell line P3X63.Ag8.653, which secretes an IgG-1 mouse-human chimeric monoclonal antibody (TVE-1). Cell density, viability, doubling time, and antibody production were used as indices to compare the efficacy of this medium with that of whole FCS medium, AIM-V (Gibco, USA) and other serum-free media. The results demonstrate that cell growth and antibody production in -GFCS medium did not differ significantly from that in FCS medium, but were significantly better than in the serum-free media (p < 0.001). TVE-1 antibody in the spent tissue culture media was purified by 50% ammonium sulfate precipitation and Protein A affinity chromatography. An antibody that was more than 99% pure was obtained. Endotoxin analysis revealed that the IgG depletion process does not generate a significant level of endotoxin in FCS (< 0.06 EU/ml).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Serum preparation and methods for the large-scale production of IgG monoclonal antibody. 785 85

There have been no reports of monoclonal antibodies reactive with vesicular monoamine transporters from any source. Western blotting and ELISA data obtained using polyclonal serum from a mouse immunized with a highly purified bovine chromaffin granule monoamine transporter preparation yielded data consistent with the presence of antibodies to the transporter. Hybridomas produced by polyethylene glycol fusion of spleen cells from the mouse with X63/Ag8.653 myeloma cells were screened in an ELISA using partially purified transporter as coating agent. Of the 1142 wells containing colonies, 14 were positive in the initial screen. Hybridomas from wells testing positive were transferred to 24-well plates, grown up, and rescreened. Those still testing positive were subcloned, and the resulting positive wells containing single colonies were grown up and stocked. Of the 6 positive clones that tolerated freeze/thaw (0.5% of the wells tested), 1 was IgG1 kappa, 2 were IgG2a kappa, and 3 were IgG2b kappa isotypes. Ascites fluid was generated in pristane-primed BALB/c mice using hybridomas that had been cloned 2-3 times, and antibodies purified on immobilized Protein A. Immunoreactivity with a mixture of these antibodies, or with only one of them, coincided with dihydrotetrabenazine (TBZOH) binding activity in fractions eluted from all columns employed in the transporter purification. Antibody from at least one of the clones was capable of removing [3H]TBZOH binding activity from a partially purified preparation of transporter. Monoclonal antibodies exhibiting these properties have not been reported previously.
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PMID:Monoclonal antibodies reactive with a monoamine transporter preparation purified from bovine adrenal chromaffin granule membranes. 804 34

Enzymatically active granule-associated serine protease ("granzyme") B has been purified from human NK cell lysates, using novel granzyme B-specific monoclonal antibodies. Two antibodies, designated 2C5 and 1D10, were produced following immunization of BALB/c mice with a nineteen amino acid peptide synthesized according to the sequence deduced from a granzyme B cDNA clone. Of several peptide-reactive culture supernatants that resulted from cell fusion of splenocytes with NS-1 myeloma cells, clones 2C5 (IgG2a) and 1D10 (IgG1) produced antibodies which detected a approximately 32kDa molecule in human NK cell lysates by Western blotting. This reactive species was detectable in lysates of IL-2-stimulated peripheral blood mononuclear cells, the human NK leukemia cell line YT, the rat NK leukemia cell line RNK-16, but not in the mouse cytotoxic T cell line CTLL-R8 or a variety of non-cytolytic hemopoietic tumor cell lines. The specificity of reactivity with granzyme B was demonstrated by the reaction of the monoclonal antibody with active granzyme in the lysate of COS-7 cells transfected with human granzyme B cDNA, but not with granzyme H expressed in an identical fashion. Western blotting on Percoll-fractionated IL-2 activated human peripheral blood lymphocyte lysates and YT demonstrated reactivity of the monoclonal antibody with a approximately 32kDa species only in those fractions with granzyme A (BLT esterase) and B (Asp-ase) activities. Moreover, 2C5/1D10 antibodies coupled to Protein A-sepharose beads immunoprecipitated enzymatically active granzyme B from YT cell lysates. Scale up of this procedure should yield a means of purifying the large quantities of natural or recombinant granzyme B required to study the function of this granzyme in cellular cytotoxicity.
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PMID:Immunopurification of functional Asp-ase (natural killer cell granzyme B) using a monoclonal antibody. 837 25

We have produced and characterized a murine-human chimeric antibody with specificity for the pre-S2 surface antigen of hepatitis B virus (HBV) in baculovirus-infected insect cells. Recombinant baculovirus carrying the cDNA coding for the heavy or light chain of the chimeric antibody was constructed and co-infected into insect cells. The chimeric antibody (BV-S2) expressed in the cells was purified by an affinity chromatography on Protein A-Sepharose 4B column and characterized by N-terminal amino acid sequencing, affinity determination for pre-S2 peptide, endoglycosidase digestion and Clq binding assay, which were then compared with those of the chimeric antibody H69K that has the same amino acid sequence as BV-S2, but produced from transfected murine myeloma cells. The N-linked glycosylation of the BV-S2 antibody was also analyzed by culturing the baculovirus-infected cells in the presence of tunicamycin. The results showed that the BV-S2 was secreted following correct removal of the leader peptides, contained N-linked carbohydrate at the heavy chain, and had the same binding affinity and Clq binding ability as H69K, suggesting that the BV-S2 chimeric antibody is functional and thus may be useful in the prevention of HBV infection.
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PMID:Characterization of a murine-human chimeric antibody with specificity for the pre-S2 surface antigen of hepatitis B virus expressed in baculovirus-infected insect cells. 857 64

Ribulose 1,5-bisphosphate carboxylase/oxygenase was purified from leaves of Zantedeschia aethiopica and used to immunize female Balb/c mice. Monoclonal antibodies (MAbs) were raised by hybridoma technology using Sp2/0 myeloma cells as fusion partner. A random selected IgG2a subclass MAb was purified from ascitic fluid by affinity chromatography on Protein A-Sepharose CL-4B, with a recovery of 84.3% and it was apparently homogeneous on native PAGE. The monoclonality of the purified MAb was determined by IEF. The MAb was highly specific for Rubisco from leaves of Z. aethiopica as determined by Western blotting and was used to determine the concentration of Rubisco protein by enzyme-linked immunoadsorbent assay (ELISA), at three distinct stages of Z. aethiopica spathe development and in the leaf. The results suggest de novo synthesis of Rubisco during the spathe regreening, which could explain, at least in part, the increase of photosynthetic activity observed during regreening.
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PMID:Production and characterization of a specific rubisco monoclonal antibody, and its use in rubisco quantification during Zantedeschia aethiopica spathe development. 1038 20

Spleen cells from BALB/c mice immunized with human thyroid stimulating hormone (beta-subunit) were fused with mouse myeloma cells (P3/X63-Ag8) and five hybridomas secreting monoclonal antibodies (MAbs) were obtained. These hybridomas specifically recognize (hTSH) and do not cross-react with the other human glycoprotein hormones such as: luteinizing hormone (LH), follicle-stimulating hormone (FSH) and human chorionic gonadotropin (hcG). The MAbs were of the IgG1 subclass and ascitic fluid from these hybridomas was purified by affinity chromatography on Protein A-sepharose CL-4B column to isolate the IgG1 active fraction. The affinity constant of these MAbs ranged from 3.2 x 10(10) to 1.5 x 10(11) M(-1).
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PMID:Production and characterization of specific monoclonal antibodies of the human thyroid stimulating hormone. 1100 7


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