Abstract
Intracellular protein phosphatase activity has been identified in the yeast Yarrowia lipolytica. This activity was maximal early in its exponential growth phase, and it was enhanced by Pi-deficiency of the culture medium. On a Pi-deficient medium, the major protein phosphatase was purified. This enzyme was dissociated with 80% ethanol treatment, its activity was slightly increased (30%) with heparine and largely enhanced (1.5 to 3-fold) with polycations. This enzyme could be classified as a type 2A protein phosphatase. It is composed of a catalytic subunit and other subunits. Its optimum pH value is 7.2, the apparent Km for casein is 37 μM and the apparent velocity 3.6 pmol hydrolyzed 32Pi min −1 pmol −1 enzyme.
Published Version
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