Abstract
Intact granules were isolated from sonicated purified rat serosal mast cells on a Percoll gradient. The granules were shown to contain a highly active phosphatidylinositol kinase that catalyzes the formation of diphosphoinositide from endogenous phosphatidylinositol in the granule membrane. The enzyme requires ATP and Mg2+ or Mn2+ for activity; Ca2+, fluoride and cyclic AMP are inhibitory. The Km for ATP is 25 microM. The initial reaction is rapid, but the response ceases within a few minutes. A comparison of the rate of phosphorylation of intact and broken membrane granules suggests that the phosphorylation occurs on the outer (cytoplasmic) surface of the granules.
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