| Literature DB >> 3100333 |
K Aktories, U Weller, G S Chhatwal.
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.Entities:
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Year: 1987 PMID: 3100333 DOI: 10.1016/0014-5793(87)81566-1
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124