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Journal Article

Photoaffinity labeling with GTP-γ-azidoanilide of a cholera toxin-sensitive 40 kDa protein from pancreatic acinar cells

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Schäfer,  Rainer
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Christian,  Anna-Luise
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Schulz,  Irene
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Schäfer, R., Christian, A.-L., & Schulz, I. (1988). Photoaffinity labeling with GTP-γ-azidoanilide of a cholera toxin-sensitive 40 kDa protein from pancreatic acinar cells. Biochemical and Biophysical Research Communications, 155(2), 1051-1059. doi:10.1016/S0006-291X(88)80603-X.


Cite as: http://hdl.handle.net/21.11116/0000-0007-E95D-B
Abstract
In isolated pancreatic acinar plasma membranes a 40 kDa protein was labeled with the photoreactive GTP-analogue [α32P]GTP-γ-azidoanilide. Increased incorporation of the photolabel into the 40 kDa protein was obtained in the presence of increasing concentrations of cholecystokinin-octapeptide (10−8 – 105 M) but not with carbachol. Adenylyl cyclase activating hormones such as vasoactive intestinal polypeptide and secretin had no effect. Pretreatment of plasma membranes with cholera toxin reduced incorporation of GTP-γ-azidoanilide into the 40 kDa protein by about 30 %. This reduction was reversed if ADP-ribosylation by cholera toxin was performed in the presence of cholecystokinin, whereas carbachol had no effect. The data indicate that a cholera toxin-sensitive 40 kDa GTP-binding protein is involved in functionally coupling cholecystokinin- but not muscarinic acetylcholine-receptors to phospholipase C.