Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin |
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Authors: | K Aktories U Weller G S Chhatwal |
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Affiliation: | 1. Rudolf-Buchheim-Institut für Pharmakologie Justus-Liebig-Universität, Frankfurter Str. 107, D-6300 Gießen, FRG;2. Institutfür Bakteriologie und Immunologie der Justus-Liebig-Universität, Frankfurter Str. 107, D-6300 Gießen, FRG |
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Abstract: | The culture medium of certain strains of Clostridium botulinum type C contains two separable ADP-ribosyltransferases. Besides the ADP-ribosylation of actin due to botulinum C2 I toxin, a second microbial enzyme causes the mono-ADP-ribosylation of a eukaryotic protein with a molecular mass of about 20 kDa found in platelets, neuroblastoma X glioma hybrid cells, S49 lymphoma cells, chick embryo fibroblasts and sperm. The eukaryotic substrate is inactivated by heating and trypsin treatment. In contrast, the novel ADP-ribosyltransferase, which can be separated by DEAE-Sephadex chromatography, is largely resistant in the short term to trypsin digestion. |
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