Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis.
Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis.
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从苏云金芽孢杆菌菌株中完全纯化磷脂酰肌醇特异性磷脂酶 C。
DOI：
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发表时间：
1983
期刊：
影响因子：
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通讯作者：
Ryo Taguchi
中科院分区：
文献类型：
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作者：
Hiroh Ikezawa;Toshikatsu Nakabayashi;Koichi Suzuki;Masahiro Nakajima;Toshiyuki Taguchi;Ryo Taguchi
从苏云金芽孢杆菌（Bacillus thuringiensis）IAM 12077的培养液中纯化出一种磷脂酰肌醇特异性磷脂酶C。纯化酶的比活力为559单位/mg，酶活力回收率为31%。对该酶的分子量（22，000）、等电点（pI = 4.9）和胞外酶释放活性进行了研究。
A phosphatidylinositol-specific phospholipase C was purified from the culture broth of Bacillus thuringiensis IAM 12077 to a homogeneous state as revealed by polyacrylamide gel electrophoresis. The specific activity of the purified enzyme was 559 units/mg and recovery of the enzyme activity was 31%. Molecular and physiological properties of the purified enzyme, including molecular weight (22,000), isoelectric point (pI = 4.9) and its ectoenzyme-releasing activity, were studied in comparison with those other known enzymes of bacterial origin.