Abstract
Recently we identified a transglutaminase (TG) activity in membranes rich in acetylcholine receptor (AChR) prepared from electric tissue of Torpedo spec (1). This activity is activated by thiol reagents (DTE) and inhibited by EGTA. It was discovered by its polymerizing effect on AChR: After few hours of incubation of receptor-rich membranes in presence of DTE SDS polyacrylamide gel electrophoresis showed that the receptorprotein did not enter the gel, after prolonged incubation not even the stacking gel (fig.1). This polymerization was not restricted to the receptor protein; other proteins, e.g. the 100 k protein supposed to be a subunit of an ATPase located in a membrane different from the receptor-rich membrane polymerized too.
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References
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© 1986 Springer-Verlag Berlin Heidelberg
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Hucho, F., Bandini, G. (1986). The Transglutaminase of Acetylcholine Receptor Rich Membranes. In: Maelicke, A. (eds) Nicotinic Acetylcholine Receptor. NATO ASI Series, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71649-2_22
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DOI: https://doi.org/10.1007/978-3-642-71649-2_22
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