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)

A high molecular weight membrane-bound DNA polymerase from the mouse myeloma, MOPC-104E, has been purified extensively, and characterized with regard to physical and reaction properties. This enzyme, which is readily distinguishable from other myeloma enzymes that are analogous to the recognized forms of cellular DNA polymerase, is ddesignated DNA polymerase III. DNA polymerase III activity in whole homogenates from MOPC-104E was solubilized and then prurifed using a series of ion-exchange chromatographic procedures followed by DNA-cellulose chromatography and glycerol gradient centrifugation; the enzyme activity as measured with poly(rA)-(dT)12-18 as template-primer and Mn2+ as divalent cation, was purified as much as 18,000-fold. In the final stages of the pruification, DNA polymerase III possessed no detectable RNA polymerase activity, nucleoside diphosphokinase activity, or nucease activity toward DNA or single- and double-stranded RNA...
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PMID:On the DNA polymerase III of mouse myeloma: partial purification and characterization. 23 42

Two species of alpha-polymerase with very similar catalytic properties have been purified to near homogeneity from a soluble protein fraction of mouse myeloma. Sedimentation analysis in 0.5 M salt-containing glycerol gradients indicated that both species had a native Mr of about 190,000. Each species contained nonidentical subunits with apparent molecular weights of about 47,000 and 54,000. Subunits of Mr = approximately 50,000 had been found previously in calf thymus alpha-polymerase (Holmes, A. M., Hesslewood, I. P., and Johnston, I. R. (1974) Eur. J. Biochem. 43, 487-499; (1976) Eur. J. Biochem. 62, 229-235). Tryptic peptide mapping failed to reveal primary structure homology between the subunits of the two enzymes. Thus, the two alpha-polymerases are clearly different species. These two enzymes are further distinguished by the fact that one of them has associated exonuclease activities. One activity degraded single-stranded DNA to mononucleotides in the 3' leads to 5' direction and acted distributively. The other exonuclease activity also degraded single-stranded DNA to mononucleotides, but this degradation was in the 5' leads to 3' direction in a processive fashion. Both exonuclease activities co-migrated with the polymerase activity during the final purification step of polyacrylamide gradient gel electrophoresis, which yielded the essentially homogenous alpha-polymerase, and also during sedimentation of the purified enzyme through a high salt glycerol gradient.
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PMID:Mouse DNA polymerase alpha. Subunit structure and identification of a species with associated exonuclease. 50 Jun 66

Two monoclonal antibodies against staphylococcal lipoteichoic acid (LTA) were made by fusing P3X63Ag8 myeloma cells and splenocytes from mice immunized with purified LTA. Both were isotyped as being IgM kappa. Their specificities were determined by enzyme-linked immunosorbent assays indicating that both antibodies reacted with the glycerol-phosphate backbone, while one of them also had some affinity for the alanyl substituent. Antibodies in serum from 7 multiple sclerosis (MS) patients and serum and cerebrospinal fluid (CSF) from 7 non-MS patients apparently reacted with the sugar moiety of LTA. In contrast, CSF antibodies from 6 of the 7 MS patients and 1 of the 7 non-MS patients had affinity for the alanine residue. This non-MS patient also had serum antibodies against the alanine residue. None of the other sera tested appeared to contain such antibodies.
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PMID:Antibodies to lipoteichoic acid from Staphylococcus aureus. Specificity of murine monoclonal and human antibodies. 242 61

Treatment of the eukaryotic organism Tetrahymena with various types of DNA-damaging agents has been reported to cause a 35-fold induction of a mitochondrial DNA polymerase. We here report that the enzyme can be induced in large-scale cultures by exposure of the cells to thymine starvation and/or intercalating agents. The induced DNA polymerase has been purified to near homogeneity, with a specific activity of approx. 300,000 units/mg protein. The relative molecular mass of the active form of the enzyme is approx. 100,000, as determined by glycerol gradient sedimentation. The subunit structure has been analysed by SDS polyacrylamide gel electrophoresis of the highly purified preparation and by immunoprecipitation with a monoclonal antibody directed to the DNA polymerase. A polypeptide of Mr 47,000 has been observed to be a subunit of the enzyme. This corresponds to the size of the subunits suggested for mitochondrial DNA polymerase from chicken embryos and mouse myeloma cells.
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PMID:Purification and characterization of an inducible mitochondrial DNA polymerase from Tetrahymena thermophila. 381 2

Three monoclonal antibodies to avian lipoprotein lipase have been isolated by fusing spleen cells from immunized BALB/c mice with myeloma P3X-63 Ag 8. The antibodies were detected by their ability to bind immobilized lipoprotein lipase in enzyme-linked immunosorbent assay (ELISA) and by immunoprecipitation of purified enzyme in the presence of second (rabbit anti-mouse) antibodies. Two of these antibodies, CAL1-7 and CAL1-11, inhibited catalytic activity, whereas with CAL1-2 interaction with lipoprotein lipase could be demonstrated only in ELISA and in Western blot assays following denaturation of the enzyme with sodium dodecyl sulfate. An immunoadsorbent column was prepared by coupling immunopurified CAL1-11 to Sepharose-4B. When acetone powder extracts of adipose tissue were applied on the column, 70% of the catalytic activity bound to the matrix. Effective elution was achieved with 1.8 M NaCl, 40% glycerol, 5% acetone, 20 mM Chaps (3[(3-cholamidopropyl)dimethylammonio]propanesulfonate), 0.5 mM EDTA, 1 mM phosphate (pH 6.5). After concentration of the active fractions on a heparin-Sepharose 4B column, the purified enzyme was obtained with an overall recovery of 25%. Sodium dodecyl sulfate polyacrylamide gel electrophoresis demonstrates that the preparation is homogeneous with a major band at Mr 60900. Thus, avian adipose lipoprotein lipase has been purified by a one-step immunoaffinity followed by a concentrating step on heparin-Sepharose 4B.
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PMID:Monoclonal antibodies to avian lipoprotein lipase. Purification of the enzyme by immunoaffinity chromatography. 404 71

C-type particles produced by a tissue culture-adapted BALB/c myeloma were characterized. It was determined that although the particles were morphologically and antigenically similar to murine leukemia and sarcoma virus, the size of their RNA was different, they lacked RNA-dependent DNA polymerase, they were unstable in NET buffer, sucrose and citrate but were stable in glycerol and Earle balanced salt solution, and they behaved differently from oncornaviruses when treated with ether and detergent.
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PMID:Characterization of C-type particles produced by a tissue culture-adapted murine myeloma. 412 86

An RNA-dependent DNA polymerase was isolated from purified virions of endogenous oncornaviruses released by the MOPC-315 murine myeloma cell line. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the purified enzyme was found to consist of two major polypeptides with molecular weights of about 28,000 and 26,500. The active enzyme had a molecular weight of approximately 56,000, as calculated from its sedimentation on glycerol density gradients, indicating that it is probably a dimer of the two subunit polypeptides. The isolated MOPC-315 virus polymerase exhibited all three activities known to be found in the DNA polymerase from oncornaviruses, namely, an RNA-dependent DNA polymerase, a DNA-dependent DNA polymerase, and an RNase H. The RNA-dependent polymerase activity showed a prounced preference for Mn2+ over Mg2+, whereas the DNA-dependent and RNase H reactions were catalyzed by these two cations to an almost equal extent. The purified polymerase was found to be immunologically related to the polymerase of Rauscher murine leukemia virus.
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PMID:RNA-dependent DNA polymerase of an endogenous type C virus of mice: purification and partial characterization. 615 78

Splenic cells from one BALB/c mouse and one C57/BL mouse, immunized with purified rat liver glucocorticoid receptor (GR), were fused with the mouse myeloma cell line Sp 2/0-Ag 14. Screening for production of anti-GR-antibodies by the hybridomas was carried out with an enzyme-linked immunosorbent assay, using partially purified rat liver GR as antigen. Further screening was by a second-antibody immunoprecipitation assay using [3H]triamcinolone acetonide-GR complex from rat liver cytosol as tracer. Hybridomas from 10 different microplate wells, positive in both assays, were successfully cloned by the limiting dilution method to monoclonality. The different origins of the monoclonal antibodies were confirmed by their various isoelectric points when analyzed by isoelectric focusing. Four of the monoclonal hybridoma cell lines secreted IgM antibodies; two, IgG1; three, IgG2a; and one, IgG2b. The GR-antibody complex was identified in glycerol density gradients by a shift of the 4S GR to an 8.5S or 19S GR-antibody complex when incubated with monoclonal IgG or IgM antibody, respectively. The 10 monoclonal antibodies recognized different determinants on the GR, all situated on that domain of the receptor that is separate from the ligand and DNA-binding domains. Also, the cross-reactivity to the mouse liver GR varied among the monoclonal antibodies. No cross-reactivity was observed to the human lymphocytic GR. NaDodSO4 electrophoresis of a 0.5% pure GR preparation followed by immunoblotting using one of the monoclonal antibodies identified a single peptide with a molecular weight of 94,000, identical to the purified rat liver GR.
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PMID:Monoclonal antibodies against the rat liver glucocorticoid receptor. 620 Aug 80

Methods using conventional Fourier transform 1H n.m.r. spectroscopy at 250 MHz for the determination of the overall deuteration levels of cells cultured in media containing 2H2O or deuterated carbon sources are described. These were developed for Escherichia coli as a model, and extended to Neurospora crassa hyphae and mouse myeloma cells P815. The results were investigated by 1H n.m.r. and neutron scattering measurements on deuterated proteins that were obtained from E. coli. It is concluded that 1H n.m.r. is able to observe the soluble proteins of E. coli in certain cases, that deuteration levels can be determined by 1H n.m.r. for small quantities of proteins in their native state, and that glycerol is a more efficient carbon source than glucose for the deuteration of E. coli proteins.
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PMID:Estimation of deuteration levels in whole cells and cellular proteins by 1H n.m.r. spectroscopy and neutron scattering. 646 29

A series of monoclonal antibodies has been prepared against the base excision repair enzyme uracil DNA glycosylase isolated from human placenta. Spleen cells from BALB/c mice immunized with purified human placental uracil DNA glycosylase were fused with either P3X63 Ag8.653 or SP2/0 myeloma cells. Hybridomas producing antibodies directed against the placental glycosylase were identified in an enzyme-linked immunosorbent assay. Each positive hybridoma was cloned twice by limit dilution and tested for anti-glycosylase activity in an enzyme immunoprecipitation assay. Each of the four clones examined in detail precipitated enzyme activity in an immunoprecipitation reaction only in the presence of rabbit anti-mouse IgG as a second antibody. No anti-uracil DNA glycosylase activity was observed in a spontaneous hybridoma used as a control. Each monoclonal antibody immunoprecipitated uracil DNA glycosylases isolated from several human tissues. Partial crossreactivity was observed with rat liver glycosylase and with a hamster enzyme. In contrast, no crossreactivity was observed with yeast or Escherichia coli glycosylase. Glycerol gradient sedimentation analysis demonstrated that one of the antibodies bound to the glycosylase at a site that did not diminish its catalytic activity. A second monoclonal antibody bound at a determinant that affected catalytic activity. Analysis of antibody-glycosylase interactions suggests that human cells contain antigenically distinct glycosylase species that may be encoded by individual uracil DNA glycosylase genes. The potential use of these monoclonal antibodies in studies examining the regulation of glycosylase isoenzymes during cell proliferation in normal human cells and in cells from cancer-prone individuals is considered.
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PMID:Isolation and characterization of monoclonal antibodies directed against the DNA repair enzyme uracil DNA glycosylase from human placenta. 657 57


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