The role of phosphorylase in the inhibitory effect of EDTA and ATP on liver glycogen synthase phosphatase. |
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| Authors: | M Laloux H G Hers |
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| Affiliation: | 1. Laboratoire de Chimie Physiologique, Université de Louvain, B-1200 Brussels, Belgium;2. International Institute of Cellular and Molecular Pathology, U.C.L. 75.39, 75 avenue Hippocrate, B-1200 Brussels, Belgium |
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| Abstract: | The work of Gilboe and Nuttall on the inhibition of liver synthase phosphatase activity by EDTA (J. Biol. Chem., 253, 4078–4081, 1978) and by ATP (Biochim. Biophys. Acta, 338, 57–67, 1974) has been confirmed and extended. It appears that these inhibitory effects are not specific since they can be elicited by other polyvalent anions and that they are transient since they last only as long as phosphorylase a is present. The duration of these inhibitory effects can be shortened by the addition of glucose or caffeine which stimulate phosphorylase phosphatase activity. It is concluded that the inhibitory effects of EDTA and ATP are mediated by phosphorylase a. |
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