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)

We have used an immunofluorescence inhibition assay to identify 2 BALB/c plasmacytomas, TEPC-1017 and TEPC-1033, that secrete large quantitites of IgD. Both TEPC-1017 and TEPC-1033 myeloma proteins bound to anti-kappa as well as hybridoma and heterologous anti-delta antibodies, but not to anti-mu, gamma, alpha, or lambda antibodies. Both myeloma proteins were purified by (NH4)2SO4 precipitation, ion exchange chromatography, gel filtration, and Staphylococcus aureus Protein A absorption. These IgD kappa myeloma proteins were used to prepare affinity purified rabbit antibodies to delta-chain and the TEPC-1017 and TEPC-1033 idiotypes. Native TEPC-1017 and TEPC-1033 both had mobilities between those of mouse IgA kappa dimers and trimers when analyzed by polyacrylamide gradient gel electrophoresis. Both IgD myeloma proteins broke down under mild reducing conditions into subunits with electrophoretic mobilities slightly slower than those of an IgA kappa monomer. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of reduced TEPC-1017 and TEPC-1033 demonstrated kappa-chains and heavy chains that co-migrated with alpha chain. These data suggested that secreted IgD contains 2 delta 2 kappa 2 subunits that are linked by an easily reducible disulfide bond. The kappa-chains of IgD secreted by TEPC-1017 and TEPC-1033 have apparent m.w. of approximately 63,000 daltons, whereas the apparent m.w. of intracytoplasmic delta-chain, intracytoplasmic delta-chain synthesized in the presence of tunicamycin, and the cellfree translation product of TEPC-1017 delta-chain mRNA are 54,000, 43,000, and 44,000 daltons, respectively. This is compatible with the interpretation that the delta-chain peptide has a leader sequence and is N-glycosylated during or shortly after peptide synthesis and is glycosylated further shortly before IgD secretion.
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PMID:IgD-secreting murine plasmacytomas: identification and partial characterization of two IgD myeloma proteins. 677 22

A factor in normal serum that selectively and reversibly inhibits proliferation of cells in culture has been enriched 160-fold from calf serum by sequential ammonium sulfate precipitation, gel filtration, and lectin-affinity chromatography. DNA synthesis of normal (but not transformed) rat hepatocytes, human lymphoblast lines, and mitogen-stimulated murine spleen cells is inhibited by greater than 90%, and Vero, murine myeloma, MELC, and a human colon carcinoma cell line to a lesser extent. Growth of other cell lines tested was not affected. Responsive cells are arrested apparently in G1 by this inhibitor, the effect of which is maximal by 24 hr and is spontaneously reversible thereafter unless it is renewed. The active fraction is a protein that migrates with the alpha 2-globulins; it is not a lipoprotein, and it is of high apparent molecular weight.
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PMID:A selective inhibitor of cell proliferation from normal serum. 692 35

Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration. The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration. The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively. After beta-elimination several oligosaccharides were separated by a combination of ion-exchange chromatography and gel-filtration chromatography. The complete structure of four of these oligosaccharides was determined by methanolysis, methylation and mass spectrometry. The structure of the four oligosaccharides which are linked to serine or threonine residues of the hinge region are as follows: beta-Gal-(1 leads to 3)-GalNAc-ol; alpha-HeuAc-(2 leads to 3)-beta-Gal-(1 leads to 3)-GalNAc-ol; beta-Gal-(1 leads to 3)-[beta-GlcNAc-(1 leads to 6)]-GalNAc-ol; beta-Gal-(1 leads to 3)-[beta-Gal-(1 leads to 4)-beta-GlcNac-(1 leads to 6)]-Gal-NAc-ol. These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
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PMID:Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk. 721 51

Monoclonal antibodies (mAbs) of IgG1 class produced by hybridomas raised with NS-1 myelomas, which were purified homogeneously by anion-exchange high-performance liquid chromatography (HPLC), contained two types of immunoglobulin light (kappa) chain. Since NS-1 myeloma synthesizes the light (kappa) chain, the mAb was presumed to be the mixture of hybrid mAbs formed by the random association of heavy (gamma l) and light chains from antigen-immunized spleen cells and light chain from NS-1 cells. Hydrophobic interaction HPLC using TSKgel Phenyl-5PW was applicable to separate 3 species of hybrid mAb from mAb fractions obtained by anion-exchange HPLC. mAbs in the fractions were adsorbed onto the gel equilibrated with phosphate-buffered saline containing 1 M ammonium sulfate and eluted by reducing the concentration to 0 M. The hybrid mAbs were purified separately. The hydrophobic interaction HPLC could discriminate a small difference in hydrophobicity between kappa chains from spleen and NS-1 cells. The immunoreactivities of hybrid mAb bearing light chains only from spleen cells and that bearing those from both spleen and NS-1 cells were almost the same, and hybrid mAb bearing light chains derived only from NS-1 cells showed a relatively lower immunoreactivity than the others. The method described here could be useful for purification of hybrid mAbs.
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PMID:Purification of monoclonal antibodies with light-chain heterogeneity produced by mouse hybridomas raised with NS-1 myelomas: application of hydrophobic interaction high-performance liquid chromatography. 750 10

A model for transport of ammonia and ammonium ions across cell membranes is presented. The model suggests that ammonium ions compete with potassium ions for inward transport, over the cytoplasmic membrane, via potassium transport proteins like the Na+/K(+)-ATPase and the Na+K+2Cl(-)-cotransporter. It also explains the difference between the ammonia/ammonium that is added to the cells and which is formed by the cells during metabolism of amino acids, especially glutamine and glutamate. The ammonium transport and subsequent events lead to predictable intracellular and extracellular pH (pHe) changes. Experiments which verified the model and the predicted consequences were performed by measurements of the pHe in concentrated cell suspensions. Addition of ammonium ions caused a time-dependent pHe increase which was inhibited by potassium ions. The test system is not per se specific for transport measurements but the effect of potassium ions on the pHe strongly favors our suggested model. Simple diffusion of ammonium ions would not be counteracted by potassium ions. The results show that ammonium ion transport in the murine myeloma cell line (Sp2/0-Ag14) used is inhibited by an excess of potassium ions. Results from experiments with specific inhibitors of suggested transport proteins were not conclusive. It is postulated that one important toxic effect of ammonia/ammonium is an increased demand for maintenance energy, caused by the need to maintain ion gradients over the cytoplasmic membrane. The results also suggest that potassium ions can be used to detoxify ammonia/ammonium in animal cell cultivations.
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PMID:Mechanisms of ammonia and ammonium ion toxicity in animal cells: transport across cell membranes. 776 10

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

Three hybridoma cell lines producing monoclonal antibodies (McAbs) against porcine serum E receptor (PSER) were established by fusing mouse myeloma SP2/o cells with spleen cells of BALB/c mouse immunized with PSER. The ascites McAbs were purified by ammonium sulfate precipitation and DEAE-cellulose chromatography. The McAbs were found to belong to the IgG1 and IgG2b subclasses, respectively. These McAbs inhibited reverse E-rosette formation and enhanced or depressed lymphocyte proliferation induced by PHA or ConA. The specificity of these McAbs was proved by immuno-dot blot and Western blot assay. The potential application of these McAbs in the study of structure and biological function of the E-receptor is discussed.
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PMID:[Study on monoclonal antibodies against porcine serum E receptor]. 790 18

A routine blood analysis, using the Hitachi 717 analyser, of an asymptomatic patient with multiple myeloma revealed a phosphate concentration of 6.2 mmol/l (reference range 0.8-1.4 mmol/l). There was no clinical or biochemical evidence for secondary hyperphosphataemia. Two additional myeloma patients with a normal renal function were found to have serum phosphate concentrations of 5 and 4.7 mmol/l. Globulin-depleted sera of these patients were found to have phosphate levels within the normal range as assayed by a Hitachi 717. All these patients were found to have normal inorganic phosphate levels when a SMAC autoanalyser was used, thus indicating spurious readings by the Hitachi 717. The incidence of pseudohyperphosphataemia in 298 patients with normal renal function and hyperglobulinaemia was 8%. To test the direct effect of globulin on phosphate analysis by the Hitachi 717, globulin was precipitated from serum of myeloma and non-myeloma patients by ammonium sulphate. The analysed data showed a positive correlation between globulin concentration and the spurious phosphate levels. Furthermore, even when inorganic phosphate was completely removed from the tested samples, spurious phosphate readings were detected in the presence of globulins from either myeloma or non-myeloma patients by Hitachi 717. It can be concluded that the ammonium molybdate method for determining inorganic phosphate in the Hitachi 717 gives spuriously high phosphate levels in the presence of a high serum globulin concentration.
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PMID:Pseudohyperphosphataemia incidence in an automatic analyzer. 798 38

The D variant of the encephalomyocarditis (EMC-D) virus is diabetogenic in mice by infecting and destroying pancreatic beta cells, but the EMC-B and EMC-DV viruses are not diabetogenic. We have presumed that the nondiabetogenicity of EMC-B and EMC-DV is mainly caused by release of some viral inhibitory factors from lymphocytes or phagocytic cells. Mice were infected with EMC-B and their splenocytes were fused with myeloma cells. The splenocyte hybridoma 12D8 releases the viral inhibitory substance (VIS) which is neither immunoglobulin nor interferon. VIS has inhibitory effects against EMC-D in several kinds of cell lines, and against EMC-D, EMC-B, coxsackie B4, reovirus and the vesicular stomatitis virus in the L cell. VIS has a strong preventive effect (100%) against EMC-D induced diabetes in SJL/J mice and DBN/2N mice. In both pre- and post-treatment studies, VIS remarkably decreased the incidence of both illness and death in SJL/J mice infected with the EMC-D virus. VIS, culture supernate itself of hybridoma, had viral inhibitory activities equivalent to 10(6)-10(7) IU/ml of interferon. VIS was very labile to heat (75% loss of activities at 37 degrees C for 18 h), stable only at pH 5-9, and precipitated at 50% (NH4)2SO4 solution. VIS activities existed in supernatant and pellet prepared from ultracentrifugation, but the properties of their activities could be differentiated quantitatively and qualitatively. It is speculated that VIS may be composed of at least two factors even though interferon may partially participate in one component of supernatant. The prevention and treatment effect of VIS on EMC-D infection in SJL/J mice might be due to the inhibition of the virus replication by VIS.
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PMID:Characterization of viral inhibitory substance released from fused splenocyte. 916 27

Spleen cells from BALB/c mice immunized with human breast cancer serum antigen were fused with murine myeloma SP 2/0 cells. After screening with ELISA and limited-dilution cloning, one hybridoma which could stably secrete specific antibody was obtained and designated McAbGB2. The titer of McAbGB2 was up to 1.2 x 10(6) after purified by ammonium sulfate and DEAE-cellulose. The McAbGB2 was defined as murine IgG1 by agarose double immunodiffusiong. Immunoblotting analysis revealed that the antigens with molecular weights of 116 kd and 45 kd recognized by McAbGB2 were distributed in human breast cancer tissue and serum.
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PMID:[Preparation and identification of monoclonal antibody GB2 directed against human breast cancer serum antigen]. 938 24


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