Inhibition of the pancreatic microsome enzyme release phenomenon by inhibitors of signal peptidase activity |
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Authors: | Linda M. Tabe Brian K. May William H. Elliott |
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Affiliation: | Department of Biochemistry, The University of Adelaide, Adelaide, South Australia 5001 Australia |
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Abstract: | ![]() The protease-sensitive release of α-amylase from rat pancreatic microsomes, incubated at 37°C, was inhibited by protease inhibitors which have been reported to inhibit signal peptidase activity. Protease inhibitors which did not affect signal peptidase activity also failed to inhibit amylase release from microsomes. Although the observed amylase release was in the opposite direction to enzyme secretion and involved fully-synthesised proteins, rather than nascent peptides, it is proposed that the enzyme release phenomenon reported from this laboratory (Pearce et al. (1978) Biochem. J. 176, 611–614) is related to the protein transporting mechanism involved in secretion. |
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Keywords: | tosyl-l-lysine chloromethyl ketone TPCK L-l-tosylamide-z-phenylethylchloromethyl ketone PMSF phenylmethane sulphonyl fluoride Absorbance at 620 nm |
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