Spanner S, Ansell G B
Biochem J. 1982 Dec 15;208(3):845-50. doi: 10.1042/bj2080845.
The highest activity of glycerophosphocholine phosphodiesterase (EC 3.1.4.2) in subcellular fractions of rat forebrain was found in the microsomal fraction though significant amounts were found in fractions containing plasma membranes. With the use of Ca(2+)/EGTA and Ca(2+)/EDTA buffers it was shown that very low concentrations of free Ca(2+) (EC(50)approx. 10(-9)m) could activate the enzyme.
在大鼠前脑亚细胞组分中,甘油磷酸胆碱磷酸二酯酶(EC 3.1.4.2)的最高活性存在于微粒体组分中,不过在含有质膜的组分中也发现了大量该酶。使用Ca(2+)/EGTA和Ca(2+)/EDTA缓冲液表明,极低浓度的游离Ca(2+)(EC(50)约为10(-9)m)就能激活该酶。