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Clostridium botulinum type C produces a novel ADP‐ribosyltransferase distinct from botulinum C2 toxin
Author(s) -
Aktories Klaus,
Weller Ulrich,
Chhatwal Gursharan S.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81566-1
Subject(s) - clostridium botulinum , trypsin , botulinum toxin , toxin , enzyme , biochemistry , chemistry , adp ribosylation , biology , microbiology and biotechnology , nad+ kinase , neuroscience
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 × 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.