Tria E, Scapin S, Cocco C, Luly P
Biochim Biophys Acta. 1977 Jan 24;496(1):77-87. doi: 10.1016/0304-4165(77)90116-7.
Adenosine 3',5'-cyclic monophosphate phosphodiesterase (EC 3.1.4.17) has been investigated in rat liver as to its insulin sensitivity. Hormone action has been assayed in vitro on a liver homogenate purified by DEAE-cellulose column chromatography, on isolated hepatocytes, on isolated plasma membranes. The DEAE-cellulose chromatography purified homogenate showed no sensitivity to insulin, whereas isolated hepatocytes incubated in presence of insulin showed increased phosphodiesterase activity in a plasma membrane-containing fraction. The plasma membrane-bound enzyme, which shows both high and low affinity components, was significantly stimulated after hormonal treatment; this effect being dependent on a V increase of the low Km form.
已对大鼠肝脏中的3',5'-环磷酸腺苷磷酸二酯酶(EC 3.1.4.17)的胰岛素敏感性进行了研究。已在体外对经DEAE-纤维素柱色谱纯化的肝脏匀浆、分离的肝细胞、分离的质膜进行了激素作用测定。经DEAE-纤维素色谱纯化的匀浆对胰岛素不敏感,而在胰岛素存在下孵育的分离肝细胞在含质膜的部分中显示磷酸二酯酶活性增加。质膜结合酶具有高亲和力和低亲和力成分,激素处理后受到显著刺激;这种效应取决于低Km形式的V增加。