Phosphatidylinositol synthase from canine pancreas: solubilization by n-octyl glucopyranoside and stabilization by manganese.
Phosphatidylinositol synthase from canine pancreas: solubilization by n-octyl glucopyranoside and stabilization by manganese.
复制标题
来自犬胰腺的磷脂酰肌醇合酶:通过正辛基吡喃葡萄糖苷增溶并通过锰稳定化。
DOI:
10.1021/bi00315a039
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发表时间:
1984
期刊:
影响因子:
2.9
通讯作者:
Hokin-Neaverson,M
中科院分区:
文献类型:
--
作者:
Parries,GS;Hokin-Neaverson,M
Gregory S. Parries and Mabel Hokin-Neaverson** abstract: Phosphatidylinositol synthase (CDP-l, 2-diacyl-i «-glycerol:» y> o-inositol 3-phosphatidyltransferase) is active in mammalian pancreas, where it plays a role in the resynthesis of phosphatidylinositol (PI) duringagonist-stimulated inosi-tol-phospholipid metabolism. The enzyme was found to be present in relatively high specific activity [30 nmol of PI formed min" 1 (mg of protein)" 1] in dog pancreas microsomal membranes, and its activity in these membranes was partially characterized. The Km for myoinositol was 0.76 mM, and the apparent Km for cytidine (5') diphospho-1, 2-diacylglycerol (CDP-diacylglycerol) was 18 µ. The apparent Ka values for activation byMn2+ and Mg2+ were respectively 42 µ and 2.5 mM. The pH optimum was 8.5-9.0. The enzyme was solubilized in stable form and in nearly quantitative yieldwith 40 mM n-octyl glucopyranoside (OG), with 4-6 mg of OG/mg