Abstract
Phosphatidylinositol 4-phosphate 5-kinase is associated with bovine brain microsomes to an extent of approximately 65% of the total cellular enzyme activity. This membrane-associated kinase activity can be solubilized with Triton X-114. Following polyacrylamide gel electrophoresis in the presence of SDS the enzyme can be renaturated from gel slices in the presence of desoxycholate and Triton X-100. Catalytic activity appears at an apparent molecular weight of 80 k. Analysis of the reaction product formed by the 80 k protein reveals the existence of a 5-phosphotransferase, identifying the 80 k polypeptide as a new phosphatidylinositol 4-phosphate 5-kinase isoform.
Published Version
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