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)

Legionellae are widely spread in natural and man-made habitats. In many instances contaminated tap water has been linked to sporadic or endemic cases of human pulmonary infections, but it is not known why, in spite of frequent occurrence, legionellae only rarely cause disease. Monoclonal antibodies against Legionella pneumophila serogroup 1 (Philadelphia 1) were prepared in order to distinguish between subtypes of this serogroup. Balb/c mice were immunized i.v. three times with heat inactivated bacteria. Antibody formation was detected by an enzyme-linked immunosorbent assay (ELISA) technique using peroxidase-conjugated antimouse IgG. Spleen cells were then fused with NS-1 myeloma cells and cloned by limiting dilution. Four monoclonal antibodies were studied in detail. The study included 47 strains of L. pneumophila: 19 strains were of human origin and 28 were isolated from different environmental sources. Most were from tap water, but none from natural habitats. All strains belonged to serogroup 1 as defined by direct immunofluorescence (DFA) using monospecific FITC-labelled polyclonal antisera from rabbits. The strains were further characterized by beta-lactamase production, activity of catalase, oxidase and proteases, analysis of ubiquinones, and demonstration of membrane protein patterns by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. A strong homogenicity between all the strains could be revealed by these methods independent of their origin. One of the monoclonal antibodies (B-1) was able to distinguish between human and environmental isolates. Eighteen of the 19 human strains reacted very strongly in DFA using antimouse immunoglobulin. No reaction, however, was seen with all of the environmental strains. Immunoblots were performed for characterization of the distinguishing feature using membrane complexes of all strains on nitrocellulose strips. The blots were incubated with antibody B-1, and immune complexes were detected by 125I-protein A. Broad intense blackening was seen between 22 and 70 kilodalton. This result suggests that no single protein, but rather a smaller component such as an oligosaccharide attached to constituents of different molecular weights, might be responsible for the discriminating reaction.
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PMID:Discrimination between clinical and environmental strains of Legionella pneumophila by a monoclonal antibody. 353 65

Ten hybridomas which produced monoclonal antibodies against species-specific cephalosporinase of Pseudomonas aeruginosa were constructed by somatic cell fusion of SP-2/0 myeloma cells with spleen cells from hyperimmunized BALB/c mice and intraperitoneally injected into mice. Monoclonal antibodies were partially purified from ascites fluids. All ten antibodies thus prepared were IgG immunoglobulins. In a solid-phase immunoassay the antibodies gave positive reactions which could be prevented by the presence of free cephalosporinase. When the antibodies were precipitated with anti-(mouse IgG), the cephalosporinase activity was co-precipitated. Also, these antibodies were co-eluted with cephalosporinase activity in gel filtration. Nine of the monoclonal antibody preparations elevated the cephalosporinase activity by about 6-40% and only one inhibited it by about 50%. All the monoclonal antibodies were highly specific to P. aeruginosa cephalosporinase and showed no cross-reaction with nine cephalosporinases and four penicillinases of other gram-negative bacteria.
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PMID:Monoclonal antibodies against species-specific cephalosporinase of Pseudomonas aeruginosa. 391 63

When a cDNA coding for the kappa light chain (L-321) from the mouse MOPC321 myeloma was cloned into Escherichia coli, L-321 antigens were found in both cytoplasmic and periplasmic fractions. In cells synthesizing the intact chain, starting with its signal peptide, the periplasm contained a mature-size immunoglobulin indicating that the eukaryotic signal peptide can initiate secretion and be processed. When the entire cDNA for L-321 (including its signal peptide) was inserted in the gene for bacterial beta-lactamase, processing cleaved only the first bacterial signal sequence of the hybrid protein synthesized. Removal of the beta-lactamase signal peptide was also observed with another beta-lactamase-L-321 hybrid which did not include the immunoglobulin signal peptide and the adjacent part of the variable region. The two hybrid proteins may, however, differ in their mode of secretion.
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PMID:Secretion and processing of an immunoglobulin light chain in Escherichia coli. 642 78

A C6-hemisuccinate derivative of morphine was prepared and conjugated to bovine serum albumin. High titer antibody producing spleen cells were removed and fused with myeloma cells of Sp2/0 origin. A C3-hemisuccinate derivative of morphine was prepared and conjugated to enzyme penicillinase used as a tracer molecule. A novel enzyme-linked immunoadsorbent assay was developed using this conjugate to screen and characterize the monoclonal antibody produced in these experiments. After two successive limiting dilutions, antibodies produced by 5 clones with good affinities ranging from 10(8) to 10(12) M(-1) and less cross-reaction (least for codeine and other structurally related molecules) were selected. These clones were found to be of IgG class with kappa light chain. Subclass determination showed that two of the clones produced IgG2b and three of them produced IgG1 type of antibody. Affinity purifications were performed for the selected clone (MOR-I). Purified antibody was coated onto the wells of microtiter plate. The standard curve was constructed with a sensitivity of 100 pg/mL covering up to 10 ng/mL in buffer and urine. The slope of the standard curve for selected clone in buffer and urine was calculated to be -0.7 and -0.64, respectively.
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PMID:Preparation and characterization of specific and high-affinity monoclonal antibodies against morphine. 1112 31

An active ester derivative of neopterin was prepared using 4-(N-maleimidomethyl) cyclohexan 4-carboxilic acid N-hydroxy succinimide ester (MCH-NHS), conjugated to bovine serum albumin (BSA) and injected for antibody production (for both monoclonal and polyclonal antibodies). High titer antibody producing spleen cells were removed and fused with myeloma cells of Sp2/0 origin. Neopterin was conjugated to the enzyme penicillinase by a one-step glutaraldehyde method, which was used as tracer. A novel enzyme immunoassay was developed using this conjugate to screen and characterize the monoclonal antibody (MAb) produced in these experiments. After limiting dilutions, it was found that antibody produced by one clone with a Ka value of 7.6 x 10-7 mol/L was specific for a number of structurally related molecules. This clone was found to be of IgG class and IgG2a subclass. The standard curvewas constructed with a sensitivity of 10 pg/well (100 pg/mL) covering up to 1 ng/mL.
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PMID:Characterization of a monoclonal antibody against neopterin using an enzyme-linked immunosorbent assay with penicillinase as label. 1139 30

The proteasome inhibitor, bortezomib, has antimyeloma activity even in myeloma cells refractory to multiple prior treatments. The most commonly reported adverse events in patients receiving bortezomib are sensory neuropathy, thrombocytopenia and gastrointestinal events. We report a patient with myeloma who developed pseudomembranous colitis after bortezomib treatment. Bortezomib has the boronic acid moiety which improves the specificity of proteasome inhibition and can be used as non-beta-lactam-based beta-lactamase inhibitors. This case indicates that gastrointestinal toxicities by bortezomib may be caused, in part, as a result of change in the colonization of colonic microflora.
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PMID:Pseudomembranous colitis following bortezomib therapy in a myeloma patient. 1723 15