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)

Immunochemical and chemical studies were used to monitor and evaluate the structural changes produced by an enzyme from Turbo cornutus in periodate-oxidized and Smith-degraded, human blood-group substances from ovarian cysts. After the first step of periodate oxidation and Smith degradation, two blood-group substances, JS (HLeb and N-1 (Lea), were precipitated by mouse-myeloma S117 serum, specific for terminal, nonreducing, beta-D-linked 2-acetamido-2-deoxy-D-glucosyl groups, but not by type XIV antipneumococcal horse serum specific for terminal, nonreducing, beta-D-linked D-galactosyl groups. An exoglycosidase, 2-acetamido-2-deoxy-beta-D-hexosidase (beta-N-acetylhexosaminidase) from Turbo cornutus, split off 2-acetamido-2-deoxy-D-glucose amounting to 22.5 and 20.4% of the total weight of JS and N-1 blood-group substances, respectively. After enzymic digestion, both blood-group substances precipitated with type XIV serum, and did not precipitate with S117 serum. The findings are in agreement with the structure propsed for the water-soluble, blood-group substances [Lloyd and Kabat, Proc. Natl. Acad. Sci. U.S.A., 61 (1968) 1477]. Specific enzymes can be of value in structural studies when used in conjunction with sequential periodate oxidation and Smith degradation.
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PMID:Action of 2-acetamido-2-deoxy-beta-D-hexosidase from Turbo cornutus on periodate-oxidized and Smith-degraded, blood-group HLeb and Lea substances from human, ovarian-cyst fluids. 21 37

Spleen cells from mice immunized with the human lung cancer line SK-LC-3 were fused with mouse NS-1 myeloma cells. One of the hybrid clones produced a monoclonal IgM antibody (designated F-3), detected with antimouse Ig-MHA and hemagglutination assays. This antibody was completely absorbed by O red cells and completely inhibited by low concentrations of H(O) glycoproteins and hog mucin (A + H). Bombay (Oh) red cells completely failed to absorb F-3 activity even after treatment with neuraminidase. A1, A2, A1B, A2B, and B red cells and A- and B-glycoproteins were less effective in absorbing or inhibiting F-3 activity. Other glycoproteins (including those having Lea or blood group precursor structures) showed little or no inhibitory activity. Serum from nude mice carrying F-3 hybridoma agglutinated O and A2 red cells at a titer of 1:40,000 and 1:640, respectively. A1, A1B, A2B, and B red cells were agglutinated with titers of 1:80 or less. Monoclonal antibody F-3 is, therefore, highly specific for H(O) blood group determinants.
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PMID:Mouse monoclonal IgM antibody against human lung cancer line SK-LC-3 with specificity for H(O) blood group antigen. 620 22

The rejection of cardiac xenografts in the hamster-to-rat combination is characterized by the production of IgM antibodies that result in the rapid loss of the graft. We have recently produced rat monoclonal antibodies (mAb) to hamster heart xenografts in an attempt to develop reagents for use in identifying the target antigens for this reaction and to study the nature of the genetic control of the humoral response. The monoclonals were created by the fusion of myeloma cells with splenic lymphocytes from LEW rat recipients of hamster cardiac xenografts. The hybridomas were screened for antibody production, reactivity to hamster cell surface antigens, and the ability to mediate hyperacute rejection of hamster heart xenografts. A panel of monoclonal antibodies has been identified that are capable of inducing hyperacute rejection. All of these mAbs are IgM and bind strongly to hamster vascular endothelium. None of the mAbs were lymphocytotoxic or bound to hamster lymphocytes or erythrocytes. Immunopathologic studies demonstrated that these mAbs react specifically with hamster vascular endothelium and mediate a complement-dependent humoral reaction leading to the destruction of the cardiac xenografts. One of the mAbs (designated as HAR-1) has been characterized in detail. HAR-1 detects antigens distributed in the vascular endothelium, epithelium of bronchi in the lung, small intestine, tubules of kidney, and selective components of lymphoid organs--e.g., the stromal cells of the spleen and thymic medullary epithelium. Western blot analysis of hamster heart proteins with HAR-1 showed multiple bands with two major bands migrating at 80 kDa and 48 kDa. Absorption of the HAR-1 antibody with 48 individual carbohydrate molecules demonstrated that the strongest reactivity of the antibody is with a sialyl-Lea carbohydrate antigen.
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PMID:Genetic control of the humoral immune response to xenografts. I. Functional characterization of rat monoclonal antibodies to hamster heart xenografts. 854 81