Partial purification and properties of a rat brain phospholipase.
Partial purification and properties of a rat brain phospholipase.
复制标题
大鼠脑磷脂酶的部分纯化和特性。
DOI：
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发表时间：
1979
期刊：
影响因子：
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通讯作者：
J. Kanfer
中科院分区：
文献类型：
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作者：
T. Taki;J. Kanfer
At least 90% of a membrane-bound phospholipase D was solubilized by extraction of freeze-dried rat brain with 0.8% Miranol H2M and 0.5% cholate. The bulk of base exchange reaction enzymes remained firmly bound to the particulate fraction under these conditions. The phospholipase D specific activity was enriched 240-fold by a purification protocol employing ammonium sulfate precipitation, and both Sepharose 4B and DEAE-cellulose column chromatography. The approximate molecular weight of the partially purified enzyme was calculated to be 200,000 based upon the elution profile from Sepharose 4B and Sephadex G-200 columns. The optimum pH was 6.0, and Km values for phosphatidylcholine and phosphatidylethanolamine were 0.75 mM and 0.91 mM, respectively. The enzyme activity was not dependent on the presence of divalent cation although Ca2+ and Fe2+ showed stimulatory effects.
