大鼠肾皮质中一种可水解甘油磷酸肌醇的磷酸二酯酶。
A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol.
作者信息
Dawson R M, Hemington N
出版信息
Biochem J. 1977 Feb 15;162(2):241-5. doi: 10.1042/bj1620241.
Abstract
- A phosphodiesterase, active at an alkaline pH, is present in the outer cortex of rat kidney and hydrolyses glycerylphosphorylinositol into glycerol and phosphorylinositol. Some inositol cyclic phosphate can also be formed indicating that the enzyme can act as a cyclizing phosphotransferase. 2. The enzyme is stimulated by Ca2+(2-3mM) whereas Mg2+ is inhibitory. 3. The activity is markedly stimulated by low concentrations of thiol reagents (1-2mM) such as cysteine or dithiothreitol. 4. The properties of the enzyme have been compared with glycerylphosphinicocholine diesterase (EC 3.1.4.2), which is also present in the isolated enzyme complex, and it is concluded that the enzymes have separate identities.
摘要
- 一种在碱性pH下具有活性的磷酸二酯酶存在于大鼠肾脏的外皮质中，可将甘油磷酸肌醇水解为甘油和磷酸肌醇。还能形成一些肌醇环磷酸酯，这表明该酶可作为环化磷酸转移酶发挥作用。2. 该酶受到Ca2 +（2 - 3mM）的刺激，而Mg2 +具有抑制作用。3. 低浓度的巯基试剂（1 - 2mM）如半胱氨酸或二硫苏糖醇可显著刺激该酶的活性。4. 已将该酶的特性与甘油磷酰胆碱二酯酶（EC 3.1.4.2）进行了比较，甘油磷酰胆碱二酯酶也存在于分离出的酶复合物中，得出的结论是这两种酶具有不同的特性。
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