Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
 ...
PMID:Purification and characterization of an inducible mitochondrial DNA polymerase from Tetrahymena thermophila. 381 2

A monoclonal antibody (MoAb, SK-930) of the IgG2a subclass to human pancreatic carcinoma cells (MIA-PaCa 2) was obtained by hybridization of spleen cells from immunized Balb/c mice with murine myeloma cells. SK-930 was investigated for reacting in indirect immunofluorescence on FACS against a panel comprising 12 types of different origin. SK-930 reacted with seven out of 11 tumor cells and with one PBL. Immunoperoxidase techniques (ABC method) showed that SK-930 antigen was present on pancreatic adenocarcinoma cells, but could not be detected on normal pancreatic tissue. Immunoprecipitation experiments and SDS-PAGE analysis revealed that SK-930 recognized 134K dalton peptide on tumor cells. These results suggest that SK-930 reacts with a novel pancreatic cancer-associated antigen.
 ...
PMID:[Monoclonal antibody to human pancreatic carcinoma cells]. 382 May 99

The level of IgA-alpha 1 anti-trypsin (alpha 1 AT) complex in a relatively large number of IgA myeloma sera has been determined, and compared with their content of polymerised forms of IgA. The level of the complex was the same in sera containing only monomeric IgA, some polymer and more than 50% polymer (as determined by SDS-PAGE). There was, however, a highly significant inverse correlation between the amount of IgA-alpha 1 AT complex in the myeloma sera and their content of 10S dimer (as determined by analytical ultracentrifugation). High levels of IgA-alpha 1 AT complex were also found in the small number of myeloma sera examined which contained paraprotein of the minor allotypic form of (Am2+) of the IgA2 sub-class, indicating that the lack of disulphide bonds between the heavy and light chains of this isotype has no influence on its ability to complex with alpha 1 AT.
 ...
PMID:Measurement of IgA-alpha 1 anti-trypsin (alpha 1 AT) complex in the sera of patients with IgA myelomatosis. 387 38

A monoclonal antibody (MAb) to human transitional-cell carcinoma of the bladder (TCCB) was obtained by immunization of a BALB/c mouse with formalin-fixed TCCB cells and subsequent fusion of the spleen cells with SP2-OAg14 myeloma line. GF 26.7.3 MAb was selected by indirect immunofluorescence (IIF) as reacting agent with target cells and negative with autologous lymphocytes and Epstein-Barr virus (EBV)-transformed lymphoblastoid cell-line. GF 26.7.3 reacts with a high percentage of bladder and colon carcinomas when examined by IIF and immunoperoxidase techniques and cross-reacts with a determinant expressed on neutrophilic cell lineage. The IIF analysis performed on bone marrow and peripheral blood (PB) from healthy subjects and leukemic patients and on leukemic cell lines showed that the expression of the structure detected by GF 26.7.3 is restricted to the neutrophilic cell lineage and first expressed at the promyelocytic level. Immunoprecipitation and SDS-polyacrylamide gel electrophoresis (PAGE) of 125 I-labelled membrane proteins from target cells were performed, but no bands were detected by autoradiography. In addition, pronase insensitivity and periodate sensitivity suggest the possible involvement of a carbohydrate determinant.
 ...
PMID:A monoclonal antibody to human transitional-cell carcinoma of the bladder cross-reacting with a differentiation antigen of neutrophilic lineage. 389 39

We report here the use of 'single shot' intrasplenic injection of human IgM for immunization of mice to obtain splenocytes for use in the production of hybridomas secreting antibodies against human IgM. Fusion was performed 3 days after intrasplenic injection of 20 micrograms of myeloma IgM. IgM-specific antibodies were found in 12% of the fusion wells; only 1 well contained antibodies which cross-reacted with other immunoglobulin classes. Two monoclonal antibodies (McAbs) have been fully characterized as specific for different epitopes on Fc mu. These antibodies can be used to detect IgM on the surface of human B cells by immunofluorescence and in solution by solid-phase radiobinding assay or single radial immunodiffusion. Both McAbs can also detect IgM fragments by immunoblotting from non-reducing SDS-polyacrylamide gels.
 ...
PMID:Use of 'single shot' intrasplenic immunization for production of monoclonal antibodies specific for human IgM. 391 4

kappa-Myeloma antigen (KMA) was immunoprecipitated from lactoperoxidase-radioiodinated HMy2 lymphoblastoid cells by using monoclonal antibody K-1-21 and was analyzed by SDS-PAGE. Under reducing conditions, two major subunits of Mr approximately 26,000 and Mr approximately 42,000, and minor components of Mr approximately 28,000, 31,000, and 36,000 were observed. The Mr approximately 26,000 subunit was identical to kappa-light chains from HMy2 surface IgG in apparent m.w., isoelectric point, and staphylococcal V-8 protease peptide map, but was not precipitated in association with Ig heavy chain. The Mr approximately 42,000 component was homologous to rabbit skeletal muscle actin by peptide mapping with staphylococcal V-8 protease. The cell surface origin of the immunoprecipitated antigen was confirmed by demonstrating lactoperoxidase dependence of iodination and complete removal from the cell surface after pronase treatment of viable cells. Thus, cell surface expression of KMA is the result of membrane association of non-heavy chain-linked kappa-light chains, possibly in noncovalent association with actin.
 ...
PMID:Structural analysis of the myeloma-associated membrane antigen KMA. 392 6

We have constructed and obtained expression of a chimeric human-mouse immunoglobulin gene after transfection into mouse myeloma cells. A human VDJH gene segment was joined to a mouse C kappa gene in the plasmid vector pSV2-gpt, and the construct was transfected into J558L cells by protoplast fusion. Analyses of six transformants by RIA and SDS-PAGE indicated that the chimeric protein was synthesized in large amounts in five. A kappa-specific transcript was observed by Northern blot analysis. Four out of five clones were stable producers of this chimeric chain over a period of 10 mo.
 ...
PMID:A human-mouse chimeric immunoglobulin gene with a human variable region is expressed in mouse myeloma cells. 393 Jun 9

Patients with idiopathic ulcerative colitis (UC) have a colonbound antibody (CCA-IgG) that reacts with colon tissue extracts. We have partially characterized a colonic protein that is specifically recognized by CCA-IgG. CCA-IgG was eluted from operative colon specimens from 10 patients with UC. A colon tissue-bound IgG was similarly eluted from six patients with Crohn's colitis, two with ischemic colitis, and one with diverticulitis. Purified serum IgG from patients with Crohn's disease, from normal subjects and a patient with myeloma were also used as additional controls. For detection of antigen(s), tissue extracts were prepared from 26 specimens of colon (UC, 12; Crohn's disease, 6; normal, 4; other controls, 4), 8 specimens of human normal stomach, duodenum, ileum, and liver (2 each). Tissue extracts were also prepared from rats and mice, including germ-free rat colons and rat's fetal colons. Immunorecognition of CCA-IgG to the tissue extracts was examined by affinity-column chromatography and by transblot analysis. Tissue-extracted proteins were electrophoresed in SDS-polyacrylamide gel, transferred to nitrocellulose sheet, and probed with iodinated CCA-IgG, colonic IgG from other inflammatory bowel disease patients, UC serum IgG, and control serum IgG. Although many proteins were present in colon tissue extracts, 9 of 10 CCA-IgG consistently recognized a protein of 40 kD. None of the nine IgG preparations from colon specimens of patients with Crohn's colitis and other colonic inflammatory diseases reacted with the 40-kD protein. Five of six symptomatic UC serum IgG and none of eight control serum IgG reacted with the 40-kD protein. The 40-kD protein was present in all colon specimens and it appeared to be organ specific. It was absent in mouse and rat tissues, including colon. The 40-kD protein is not actin and nor a part of the Ig molecule. These results suggest that the 40-kD protein is a colonic "autoantigen" that may initiate a specific IgG antibody response in UC.
 ...
PMID:Isolation and characterization of a colonic autoantigen specifically recognized by colon tissue-bound immunoglobulin G from idiopathic ulcerative colitis. 401 82

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.
 ...
PMID:Monoclonal antibodies to avian lipoprotein lipase. Purification of the enzyme by immunoaffinity chromatography. 404 71

The receptor for transferrin is one of the major surface proteins of proliferating lymphocytes and other cells. It binds ferrotransferrin from serum and endocytoses it into an acidic nonlysosomal intracellular compartment where iron is released, but in which apotransferrin remains tightly bound to its receptor. Recycling of the apotransferrin-receptor complex to the cell surface is associated with a return to neutral pH and concomitant loss of affinity of apotransferrin for its receptor. Apotransferrin is then free to leave the cell and initiate a new cycle. We have exploited this cycle in a novel method for the purification of the receptor for transferrin. Murine myeloma cells were lysed in nonionic detergent, and the lysate passed over a column of ferrotransferrin-agarose at pH 7.4. After washing with sodium acetate at pH 5.0, iron was removed with sodium citrate pH 5.0 and desferrioxamine. Upon returning the pH to neutrality, the receptor was eluted and found to be homogeneous by SDS-polyacrylamide gel electrophoresis under both reducing and nonreducing conditions. The degree of purification was estimated to be at least 3,000-fold, and the calculated yield was 10 to 20%. The purified receptor was capable of binding to transferrin. The receptor was digested with trypsin, and the resulting peptides were separated by reversed-phase high performance liquid chromatography in NH4HCO3. Selected peptides were rechromatographed in 0.1% trifluoroacetic acid, and their amino acid sequences were determined.
 ...
PMID:The receptor for transferrin on murine myeloma cells: one-step purification based on its physiology, and partial amino acid sequence. 609 68


<< Previous 1 2 3 4 5 6 7 8 9 10