Abstract
A PtdIns 4-kinase was purified extensively from rat liver exocytotic vesicles. The enzyme had a low K m for ATP, was inhibited by adenosine, and had an apparent molecular mass of 54 kDa, indicating it to be a type II Ptdlns-kinase. The activity of the purified enzyme was enhanced several-fold by PtdCho, and to some extent by other phospholipids with basic polar head groups, and was inhibited by PtdSer. Kinetic analyses, presenting the substrate in mixed micelles of Triton X-100, Ptdlns and PtdCho, showed that the effect of PtdCho was both to increase V max and to decrease the apparent K m for micellar PtdIns.
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