Some properties of the phosphoinositide inositolphosphohydrolase of guinea‐pig intestinal mucosa supernatant fraction are described. The enzyme has an absolute requirement for metal ions, the most efficient activator being Ca2+. The pH optimum is 5.3 in acetate buffer and 5.9 in maleate; activity is higher in the latter. The effects of detergents and various reagents are described. Corn phosphatidyl inositol is hydrolysed faster than brain phosphatidyl inositol; the fatty acid compositions of these lipids have been compared. The enzyme is remarkably specific for the phosphoinositides. The composition of the enzyme preparation has been studied. The enzyme appears to be widely distributed in animal tissues.
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Atherton et al. (1968) studied this question.
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