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PubMed · 183978

ESR-spectroscopic changes on enzymatic depolymerization of spin-labelled amylose.

R Darcy·K F McGeeney
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AmylasesAmyloseElectron Spin Resonance SpectroscopyKineticsJournal Article

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R Darcy, K F McGeeney. 1976-09-15. ESR-spectroscopic changes on enzymatic depolymerization of spin-labelled amylose.. https://doi.org/10.1007/bf01927584

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PubMed1992

Effects of calyculin A on amylase release in streptolysin-O permeabilized acinar cells.

The effects of the phosphatase inhibitors calyculin A and okadaic acid on amylase release from streptolysin-O permeabilized rat pancreatic acini were investigated. Both agents induced similar biphasic effects with moderate potentiation of calcium-stimulated amylase release at medium and strong inhibition at higher concentrations. Calyculin A was thirty times more potent than okadaic acid and at 100 nM totally inhibited calcium-induced amylase release while 3 microM okadaic acid reduced amylase release by 78%. 100nM calyculin A also completely inhibited GTP gamma S-potentiated amylase release and partially inhibited phorbol ester potentiated secretion. The data indicate that inhibition of a serine/threonine phosphatase, probably a type 1 phosphatase, leads to inhibition of calcium-induced amylase release in permeabilized pancreatic acini.

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