Abstract
The inhibitor-1 phosphatase but not the phosphorylase phosphatase activity of a newly discovered 250 kDa polycation-stimulated (PCS M) protein phosphatase in rabbit skeletal muscle is increased up to 10-fold by a Ca 2+-dependent protease. The enzyme-directed protease effect to which the PCS H and PCS L. phosphatases are insensitive was progressively lost during purification of the enzyme. This could be explained by either a slow conversion of the enzyme to an active form of the enzyme with a change in specificity, or the loss of a protease-sensitive inhibitor of the inhibitor-1 phosphatase activity, resulting in a PCS phosphatase characterized by its high inhibitor-1/phosphorylase a activity ratio. The Ca 2+-dependent protease is completely inhibited by EGTA or leupeptin.
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