Cockcroft S, Taylor J A
Biochem J. 1987 Jan 15;241(2):409-14. doi: 10.1042/bj2410409.
Fluoride and guanosine 5'-[gamma-thio]triphosphate (GTP gamma S) both activate the hepatocyte membrane polyphosphoinositide phosphodiesterase (PPI-pde) in a concentration-dependent manner. AlCl3 enhances the fluoride effect, supporting the concept that [A1F4]- is the active species. Analysis of the products of inositol lipid hydrolysis demonstrate that phosphatidylinositol bisphosphate is the major lipid to be hydrolysed. Guanosine 5'-[beta-thio]diphosphate (GDP beta S) is an inhibitor of activation of PPI-pde by both fluoride and GTP gamma S. These observations suggest that the guanine nucleotide regulatory protein (termed Gp) bears a structural resemblance to the well-characterized G-proteins of the adenylate cyclase system and the cyclic GMP phosphodiesterase system in phototransduction.
氟化物和鸟苷5'-[γ-硫代]三磷酸(GTPγS)均以浓度依赖的方式激活肝细胞膜多磷酸肌醇磷酸二酯酶(PPI-pde)。AlCl3增强氟化物的作用,支持[A1F4]-是活性物质的概念。对肌醇脂质水解产物的分析表明,磷脂酰肌醇二磷酸是主要被水解的脂质。鸟苷5'-[β-硫代]二磷酸(GDPβS)是氟化物和GTPγS激活PPI-pde的抑制剂。这些观察结果表明,鸟嘌呤核苷酸调节蛋白(称为Gp)在结构上与腺苷酸环化酶系统和光转导中的环鸟苷酸磷酸二酯酶系统中特征明确的G蛋白相似。