Saltiel A R, Doble A, Jacobs S, Cuatrecasas P
Biochem Biophys Res Commun. 1983 Feb 10;110(3):789-95. doi: 10.1016/0006-291x(83)91031-8.
Incubation of rat liver plasma membranes with insulin enhances the production of small molecular weight substances which regulate the activity of liver acetyl CoA carboxylase. While low concentrations of insulin cause the release of a carboxylase stimulator from membranes, concentrations greater than 10(-9) M generate less stimulating activity. This biphasic concentration curve for insulin can be resolved by differential alcohol extraction into two fractions which have antagonistic activity. The production of both substances is enhanced by insulin. Chemical and chromatographic evidence suggest that these substances are identical to the previously described "mediators" which regulate both pyruvate dehydrogenase and adenylate cyclase activities.
用胰岛素孵育大鼠肝细胞膜可增强小分子物质的产生，这些小分子物质可调节肝乙酰辅酶A羧化酶的活性。低浓度胰岛素会导致一种羧化酶刺激物从膜中释放出来，而浓度大于10⁻⁹ M时产生的刺激活性较低。胰岛素的这种双相浓度曲线可通过差示乙醇萃取法分解为具有拮抗活性的两个部分。两种物质的产生均受胰岛素增强。化学和色谱证据表明，这些物质与先前描述的调节丙酮酸脱氢酶和腺苷酸环化酶活性的“介质”相同。
