Further characterization of human RNase MRP/RNase P and related autoantibodies.
We characterized a panel of human RNase MRP/RNase P autoantibodies by immunoprecipitation, immunodepletion, immunoaffinity purification and immunoblotting. We report on the protein spectrum that is recognized by RNase MRP/RNase P autoantibodies. We also describe another, related patient serum that based on these assays does not immunoprecipitate RNase P/MRP/Th40. This autoantibody 'KC', however, coimmunoprecipitates the RNase MRP/RNase P associated RNAs from HeLa and La9 cell extracts as shown by nuclease protection experiments.
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D000918:Antibody Specificity; D001323:Autoantibodies; D001324:Autoantigens; D002457:Cell Extracts; D002460:Cell Line; D002467:Cell Nucleus; D004722:Endoribonucleases / Q000276:immunology*; D006367:HeLa Cells; D006801:Humans; D007106:Immune Sera; D011233:Precipitin Tests; D016337:RNA, Catalytic / Q000276:immunology*; D012333:RNA, Messenger / Q000032:analysis; D043262:Ribonuclease P
D001323:Autoantibodies; D001324:Autoantigens; D002457:Cell Extracts; D007106:Immune Sera; D016337:RNA, Catalytic; D012333:RNA, Messenger; C071036:To autoantigen; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; C468368:RPP14 protein, human; D043262:Ribonuclease P