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Query: UMLS:C0679427 (myeloblastosis)
 982 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The avian myeloblastosis virus pp19 protein was separated from the other virus proteins by a rapid and simple purification procedure which yields milligram amounts of homogeneous protein. This protein was then fragmented by digestion with cyanogen bromide. When the mixture of the cyanogen bromide peptides was passed through a 60S avian myeloblastosis virus RNA-cellulose column, only one peptide bound with high affinity to the resin. The peptide migrated on a sodium dodecyl sulfate-polyacrylamide gel with an approximate molecular weight of 2,900 and will be referred to as the p3B peptide. This peptide was also isolated directly by chromatography of the cyanogen bromide-digested pp19 protein on a reverse-phase high-pressure liquid chromatography column. It was again the only cyanogen bromide peptide of the pp19 protein that bound to the RNA affinity resin. The p3B peptide is a basic peptide, as was seen by its rapid migration on acid-urea-polyacrylamide gels and its amino acid composition. A partial amino acid sequence analysis of the p3B peptide indicated that it was derived from the amino terminus of the intact protein. Although the p3B peptide bound to 60S RNA, it did not demonstrate the selective binding of native pp19 to regions of the RNA containing secondary structure.
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PMID:Cyanogen bromide digestion of the avian myeloblastosis virus pp19 protein: isolation of an amino-terminal peptide that binds to viral RNA. 630 Apr 41

Five hybridoma cell lines which secrete antibodies to avian leukosis/ sarcoma (ALV) group-specific (gs) antigens (gag gene products) have been established. The hybrid cells resulted from fusion of P3/X63-Ag8.653 myeloma cells with splenocytes of BALB/c mice which had been immunised with purified avian myeloblastosis virus (AMV). Screening of supernatant fluids was performed by an indirect double antibody sandwich enzyme-linked immunosorbent assay (IDAS-ELISA) and the immunoelectroblotting technique. Three hybrid clones secrete monoclonal antibodies (MCA) to 27,000 dalton polypeptides (p27) and two hybridomas produce monoclonal antibody directed to 19,000 dalton phosphoprotein (pp19). All five monoclonal antibodies belong to mouse immunoglobulin isotype IgG(1). MCAs directed to different ALV-p27 epitopes can replace polyclonal rabbit or hamster anti-gs sera in the DAS-ELISA in use for the detection of congenitally ALV-shedding hens. In albumen samples a 16- to 32-fold increase of sensitivity of ALV gs-antigen detection was obtained as compared to the DAS-ELISA employing polyclonal sera. Gs-antigens of a purified AMV preparation were detectable up to minimal concentrations of 13 pg/ml.
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PMID:Application of monoclonal antibodies in the avian leukosis virus GS-antigen ELISA. 1876 97