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)

Phosphorus-31 nuclear magnetic resonance (NMR) studies on the two phosphorus nuclei of the phosphonium analogue (Me3P+CH2CH2OPO3(2-)) of phosphocholine are used to monitor the charged subsites in the phosphocholine-binding immunoglobulin A mouse myeloma M603. Comparison of the 270-MHz 1H NMR difference spectrum on addition of either this analogue or phosphocholine to M603 and the almost identical changes in the pKa values of the phosphate groups on binding to M603 confirm that the analogue is a good model for phosphocholine. The pKa of the phosphate groups is decreased by 0.5 unit on binding to M603, which is consistent with the phosphate group being hydrogen bonding to Tyr-33H and Arg-95L, as suggested from the X-ray structure, and also implies that the binding energies for the mono- and dianion are similar. The P+Me3 moiety is used to probe the electrostatic interactions in the choline subsite. Titration of the chemical shift of the phosphonium phosphorus reflects a group on the protein that has a pKa value of less than or equal to 5, which from the refined X-ray structure (D.R. Davies, personal communication) of the site is assigned to Asp-97L. The choline subsite is monitored by using 1H NMR difference spectra, which indicates that the subsite is highly aromatic as expected from the crystal structure that places Trp-107H and Tyr-100L in this subsite. The ring current interactions from these rings can account for the 1H NMR chemical shift data on choline.
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PMID:A combined proton and phosphorus-31 nuclear magnetic resonance investigation of the combining site of M603, a phosphocholine-binding myeloma protein. 629 93

To determine the cellular distribution of Toxoplasma antigens, RH strain tachyzoites were incubated with either one of three monoclonal antibodies (FMC 19, FMC 20, FMC 22) to T. gondii, or one of two controls (the murine myeloma protein MOPC 21, or phosphate buffered saline), and then incubated with peroxidase-labelled goat-antimouse IgG. Diaminobenzidine was added as substrate and electron microscopy was used to localize the reaction. All three antibodies bound to the entire periphery of the tachyzoite surface membrane. To ascertain the chemical composition of the antigens against which seven monoclonal antibodies (FMC 18, FMC 19, FMC 20, FMC 22, FMC 23, 2G11, 3E6) to T. gondii reacted, untreated, pronase-treated, or periodate-treated tachyzoites were incubated with the antibodies or MOPC 21, and then with [125I]-Protein A. The pronase-treated tachyzoites showed reduced binding for six of the antibodies, compared with the reduction in binding of MOPC 21 with the pronase-treated parasites. The periodate-treated tachyzoites had reduced binding for FMC 18 only. The results of these experiments confirm that most Toxoplasma surface antigens are protein in nature, and are consistent with the hypothesis that at least one cytoplasmic antigen is secreted onto the parasite cell surface.
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PMID:Ultrastructural and biochemical studies on the immunohistochemistry of Toxoplasma gondii antigens using monoclonal antibodies. 634 26

Monoclonal antibodies specific for aflatoxin B1, aflatoxin B2, aflatoxin M1, and the major aflatoxin-DNA adducts were obtained following fusion of mouse SP-2 myeloma cells with spleen cells of mice immunized with aflatoxin B1 covalently bound to bovine gamma globulin. The aflatoxin-modified protein used to immunize mice was produced chemically by activating aflatoxin B1 to a 2,3-epoxide derivative, which then covalently bound to the protein. One of the monoclonal antibodies isolated (2B11) was found to be a high-affinity IgM antibody with an affinity constant for aflatoxin B1, aflatoxin B2, and aflatoxin M1 of about 1 X 10(9) liters per mol. In a competitive radioimmunoassay using [3H]aflatoxin B1, 3 pmol (1 ng) of aflatoxin B1, aflatoxin B2, or aflatoxin M1 caused 50% inhibition with this antibody. The antibody also had significant cross-reactivity for the major aflatoxin-DNA adducts: 2,3-dihydro-2-(N7-guanyl)-3-hydroxyaflatoxin B1 and 2,3-dihydro-2-(N5-formyl-2',5', 6'-triamino-4'oxo-N5-pyrimidyl)-3-hydroxyaflatoxin B1. The antibody was also covalently bound to Sepharose-4B and used in a column-based solid-phase immunosorbent assay system. Aflatoxins added in vitro to phosphate buffer, human urine, human serum, or human milk at levels expected to be obtained in human samples acquired from environmentally exposed individuals were quantitatively recovered by applying the mixture to this antibody affinity column purification system. Preliminary studies using urine samples from rats injected with radiolabeled aflatoxin B1 have also indicated that aflatoxin metabolites can be isolated by these methods. Furthermore, we have found that the monoclonal antibody affinity columns can be regenerated for multiple use. Therefore, the monoclonal antibodies and their application to affinity chromatography represents a useful and rapid technique to purify environmentally occurring levels of this carcinogen and some of its metabolites for quantitative measurements.
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PMID:High-affinity monoclonal antibodies for aflatoxins and their application to solid-phase immunoassays. 644 Jan 43

A patient with multiple myeloma complicated by hypercalcemia is presented. During the state of an elevated calcium phosphate product a transient diffuse accumulation of Tc 99m MDP in the liver was demonstrable, whereas the demonstrated metastatic calcifications of the kidneys persisted after therapeutic reduction of the elevated ion product. This points to a difference in the formation of calcium phosphate precipitations in these organs. Accumulation of Tc 99m labelled bone seeking agents in the liver must not always mean severe liver damage or amyloidosis or tumour manifestation. An altered serum calcium phosphate balance has to be taken into account when interpreting scintigrams performed with bone seeking radiopharmaceuticals.
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PMID:Transient accumulation of Tc 99m MDP in the liver. 644 28

Groups of mice were given an intraperitoneal injection of one of six monoclonal antibodies to Toxoplasma gondii, a mixture of equal amounts of five monoclonal antibodies to T. gondii, or the murine myeloma protein MOPC 21, and challenged with either a highly virulent or moderately virulent parasite strain. Two monoclonal antibodies (FMC 19 and FMC 22) conferred total protection against the moderately virulent challenge, with all mice surviving, whereas 90% of control mice died. FMC 19 and FMC 22 also conferred significant protection against the highly virulent challenge as indicated by a prolonged mean time to death (MTD) of immunized compared with control groups of mice. One monoclonal antibody (FMC 23) and the mixture of five antibodies gave significant protection against the moderately virulent challenge only. Passive immunization with dilutions of FMC 22 antibody indicated that the lowest serum titer needed to confer significant protection to mice against a moderately virulent Toxoplasma challenge was 1/640. Mice challenged with highly virulent tachyzoites that had been preincubated with FMC 22 had a significantly longer MTD than mice challenged with highly virulent tachyzoites that had been preincubated with MOPC 21 or phosphate buffered saline, pH 7.2 (PBS). Immunoprecipitation and autoradiography of radiolabeled tachyzoites confirmed that FMC 19 was directed against a 35,000 molecular weight (mol. wt.) antigen and FMC 22 was directed against a 14,000 mol. wt. fraction. The potential for use of single antigens as protective immunogens in preventing toxoplasmosis is raised.
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PMID:Monoclonal antibodies to Toxoplasma cell membrane surface antigens protect mice from toxoplasmosis. 663 78

Precursor RNAs were synthesized in vitro from a plasmid in which the early region 2 (E2) of adenovirus 2 is fused to an efficient bacteriophage promoter (Salmonella phage 6). The RNAs were purified and utilized as substrates for in vitro splicing in the presence of nuclear extracts prepared from MOPC-315 mouse myeloma cells. We have shown previously (Goldenberg, C.J., PNAS, August, in press, 1984) that in vitro splicing in those extracts was accurate at the nucleotide level. We now show that: i) the new internucleotide bond at the splice junction generated in vitro is a 3',5'-phosphodiester bond; and ii) the phosphate that forms the splice between the exons is derived from the pre-mRNA.
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PMID:Characterization of the newly-formed internucleotide bond of in vitro spliced mRNAs. 674 46

In order to improve the yield of hybridomas for monoclonal antibody production, 8 different sources and molecular weights of polyethylene glycol (PEG) were compared as fusing agents. Sp2/0 myeloma cells were fused with murine splenic lymphocytes immunized with sheep red blood cells. The Kodak 1450 PEG produced the maximum number of hybridomas. The optimal technique consisted of slowly adding 1 ml of freshly prepared fusogen (5 g Kodak 1450 PEG, 0.5 ml dimethylsulfoxide, and 5 ml of phosphate-buffered saline, pH 7.0) to the cells over a 1 min period, incubating the mixture at 37 degrees C for 90 s, then gradually diluting the mixture in 50 ml of Hanks' buffered salt solution. After 10 min, the cells are centrifuged, resuspended in selective medium with feeder macrophages and cultured. This procedure routinely produces between 600-3,000 hybridomas per fusion.
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PMID:Comparison of polyethylene glycols as fusogens for producing lymphocyte-myeloma hybrids. 674 7

The case here reported of 72 year-old female with osteomalacia in whom an adult's Fanconi's syndrome with distal tubular involvement and a monoclonal IgG-lambda paraprotein were discovered. There was urinary excretion of lambda light chains without evidence of myeloma or amyloidosis. Such apparently unrelated entities might be subject to an unitary pathophysiological approach: the nephrotoxicity of light chains could cause a Fanconi's syndrome, which in turn would give rise to osteomalacia through phosphate depletion. It is noteworthy that in this patient the urinary excretion of light chains was of the lambda type, in contrast to similar cases described in the literature which presented mostly kappa chains. The likelihood of this patient developing myeloma or amyloidosis at a later stage is discussed.
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PMID:[Monoclonal IgG lambda paraprotein, Fanconi's syndrome of the adult, and osteomalacia (author's transl)]. 678 49

A murine BALB/c IgG2a (lambda 3) myeloma immunoglobulin SAPC-15 with binding activity for negatively charged polysaccharides has been purified by affinity chromatography, and its interaction with heparin and various other polyanionic antigens has been studied. The antigen-binding activity has been demonstrated to reside in the Fab part of the immunoglobulin. The S15 myeloma protein in 0.05 M Tris buffer at pH 7.4 precipitated dextran sulfate, heparin, chondroitin sulfate A, B and C, hyaluronic acid, H. influenzae type b polysaccharide, calf thymus DNA, Klebsiella polysaccharide K63 and poly-L glutamic acid. Of these antigens only dextran sulfate was precipitated in 0.01 M phosphate buffered saline (0.15M), pH 7.4. The pepsin S15 Fab fragment did not precipitate with any of these antigens. The intrinsic tryptophanyl fluorescence of S15 was changed maximally by the addition of heparin, and the binding affinity of the immunoglobulin for this antigen was high (greater than 10(6) L/M). S15 may resemble antibody molecules that react with antigens under non-physiological conditions or in pathological conditions or in the external environment as in the lumen of the gut. All the above interactions of S15 with antigens persisted in 0.05 M Tris buffer made physiologically isotonic by the addition of sucrose, and S15 could thus be used to identify these antigens on cell surfaces.
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PMID:The interaction of mouse myeloma immunoglobulin S15 with negatively charged polysaccharide antigens. 681 62

We have introduced a functionally rearranged murine kappa light chain immunoglobulin (Ig) gene into an Abelson murine leukemia virus-transformed lymphoid cell line. Plasmid pSV2gpt-kappa 41, containing the kappa light chain gene from the myeloma MOPC41 and the selectable marker gene gpt, was introduced into 81A-2 cells by the calcium phosphate coprecipitation technique. Cells expressing the gpt gene were selected by growth in medium containing mycophenolic acid. One transfected cell line, kappa-2, was shown to make kappa mRNA and polypeptide chains and to assemble the kappa chain product with gamma 2b heavy chains to form an apparently complete IgG2b. When bacterial lipopolysaccharide was added to the growth medium, levels of kappa mRNA and polypeptide increased, showing regulated expression of the introduced kappa gene.
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PMID:Regulated expression of an immunoglobulin kappa gene introduced into a mouse lymphoid cell line. 681 55


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