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)

Monoclonal antibodies to factor IX were produced by immunization of balb/c mice with purified factor IX and fusion of spleen cells with SP-1 murine myeloma cells. Antibody producing hybrids were detected by an enzyme linked immunoassay (ELISA) and by coagulation inhibitor (Bethesda type) methods. Monoclonal antibodies with titres of greater than 1 X 10(5) tested by the ELISA and 5000-8000 inhibitor units were obtained. A new ELISA method was developed using one of these monoclonal antibodies to quantitate factor IX antigen (IXAg) in plasma samples from patients with hereditary factor IX deficiency. In addition a two-site solid phase immunoradiometric assay (IRMA) for factor IX was established. The results of these new methods were compared with those obtained on the same plasma samples using conventional factor IX coagulation assays and the Laurell rocket method. The lower limit for the detection of IXAg by the ELISA was approximately 0.01 unit per ml whilst that for the IRMA was about 0.001 unit per ml (normal plasma = 1 unit per ml). The lower detection limit for IXAg using the Laurell rocket method was about 0.06 units per ml. The improved sensitivity of the new immunoassays enabled quantitation of low levels of IXAg in patients with moderately severe factor IX deficiency and confirmed the presence of excess IXAg compared to IX activity (IXC) in a relatively high proportion of cases (28 out of 51 tested). Results of testing plasma from obligate carriers confirm the suggestion that measurements of IXAg and IXC may improve the classification of carrier status in these kindred.
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PMID:Immunoassays of factor IX antigen using monoclonal antibodies. 397 Aug 58

Hybridoma producing a monoclonal antibody IgG1 to one-chain tissue plasminogen activator (t-PA) derived from human melanoma cells was obtained by fusion of mouse myeloma cells (SP-1) and spleen cells of mice previously immunized with purified t-PA. The monoclonal antibody reacted only with t-PA derived from the human melanoma cells (Bowes), and not with plasminogen activator purified from porcine heart or from human urine. The monoclonal antibody obtained from mouse ascites demonstrated 50 times stronger antibody activity than that of polyclonal antibody obtained from mouse serum. The monoclonal antibody bound t-PA firmly, inhibited the fibrinolytic activity of t-PA, but did not inhibit the amidolytic activity of t-PA completely. The fibrin-binding ability of t-PA was not inhibited. The binding of monoclonal antibody to the non-reduced form of t-PA did not differ from that to the reduced form of t-PA.
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PMID:Monoclonal antibody to human tissue plasminogen activator. 644 14

A human IgMk monoclonal antibody, 2F7, of predetermined specificity, has been produced by the fusion of human peripheral blood lymphocytes with the nonsecreting mouse myeloma line SP-1. The heterohybridoma has remained stable for over 8 mo, with culture supernatants containing up to 30 micrograms/ml of specific IgM. The antibody has been shown to be capable of inducing a blastogenic response in the absence of antigen in the peripheral blood lymphocytes of normal subjects immune to the antigen. The ability to choose an antigen, immunize a human subject to that antigen, and then use the peripheral blood lymphocytes from that subject to produce antigen-specific human monoclonal antibodies should be of great value in a wide variety of investigative, diagnostic, and therapeutic endeavors.U
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PMID:Human monoclonal anti-keyhole limpet hemocyanin antibody-secreting hybridoma produced from peripheral blood B lymphocytes of a keyhole limpet hemocyanin-immune individual. 697 16