1. Immunochemical detection of ADP-ribosylating enzymes in the archaeon Sulfolobus solfataricus
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Agata Gambacorta, Barbara Nicolaus, M. Rosaria Faraone-Mennella, and Benedetta Farina
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Male ,Thermophiles ,Blotting, Western ,ved/biology.organism_classification_rank.species ,Immunoblotting ,Biophysics ,Enzyme-Linked Immunosorbent Assay ,Biochemistry ,Sulfolobus ,Western blot ,Structural Biology ,Testis ,Escherichia coli ,Genetics ,medicine ,Animals ,Transferase ,Molecular Biology ,Polymerase ,Antibody ,ADP Ribose Transferases ,chemistry.chemical_classification ,Adenosine Diphosphate Ribose ,biology ,medicine.diagnostic_test ,ved/biology ,Thermophile ,Sulfolobus solfataricus ,Cell Biology ,biology.organism_classification ,Immunohistochemistry ,Molecular biology ,Archaea ,Molecular Weight ,Enzyme ,chemistry ,Polyclonal antibodies ,biology.protein ,Cattle ,Poly(ADP-ribose) Polymerases ,ADP-ribosylation - Abstract
Polyclonal antibodies raised against eukaryotic mono(ADPribose)transferase and poly(ADPribose)polymerase were used to test the presence of antigenic determinants in a crude extract of Sulfolobus solfataricus, a thermophilic archaeon. Samples from eukaryotic (bull testis) and bacterial (E. coli) sources were analysed for comparison. All tested antibodies reacted with the sulfolobal sample with a specificity comparable to that of the eukaryotic preparation, as revealed by ELISA test, activity assays in the presence of antibodies and immunoblot experiments. After electrophoresis and western blot of sulfolobal proteins, a band at a mass around 50 kDa was detected by immunostaining.
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