Article
Clostridium botulinum C2 toxin: binding studies with fluorescence-activated cytometry.
Toxicon : official journal of the International Society on Toxinology - 1 Aug 2002
Stiles Bradley G, Blöcker Dagmar, Hale Martha L, Guetthoff Mary Ann, Barth Holger
Abstract excerpt
Clostridium botulinum C2 enterotoxin consists of two unlinked proteins designated as C2II, which recognizes a cell-surface glycoprotein and translocates an ADP-ribosyltransferase, C2I, into the cytosol of a targeted cell. Fluorescence-activated cytometry was used to study the cellular interactions of Alexa488-labeled C2I (C2I-A488) and proteolytically activated C2II (C2IIa-A488). The binding of C2IIa-A488 (4...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
