Properties and characterization of low molecular weight inhibitor of calmodulin-dependent cAMP phosphodiesterase from rat liver.
Properties and characterization of low molecular weight inhibitor of calmodulin-dependent cAMP phosphodiesterase from rat liver.
复制标题
大鼠肝脏钙调蛋白依赖性 cAMP 磷酸二酯酶低分子量抑制剂的特性和表征。
DOI：
10.1016/0024-3205(84)90516-2
复制
发表时间：
1984
期刊：
影响因子：
6.1
通讯作者：
Solomon,SS
中科院分区：
文献类型：
--
作者：
Rao,RH;Palazzolo,M;Sanders,L;Smoake,JA;Solomon,SS
我们已经鉴定了两种不同种类的钙调素依赖性cAMP磷酸二酯酶抑制剂：1）低分子量（LMW）和2）高分子量（HMW）形式。这些抑制剂从大鼠肝脏中提取。低分子量和高分子量抑制剂均为热稳定性酸性抑制剂，在长期储存和/或反复冻融后会失去活性。低分子量抑制剂已纯化至约7，000倍，回收率为300%。LMW抑制钙调蛋白依赖性cAMP磷酸二酯酶，与钙调蛋白的来源无关（例如脂肪、脑、心脏、红细胞）。LMW本质上似乎是脂质，分子量为1，500 - 5，000。这些抑制剂在糖尿病中的作用和胰岛素的作用机制。
We have identified two different species of inhibitors of calmodulin-dependent cAMP phosphodiesterase: 1) a low molecular weight (LMW) and 2) a high molecular weight (HMW) form. These inhibitors are extracted from rat liver. Both LMW and HMW inhibitors are heat-stable, acidic in nature and lose activity with prolonged storage and/or repeated freezing and thawing. The low molecular weight inhibitor has been purified to about 7,000-fold with 300% recovery. LMW inhibits calmodulin-dependent cAMP phosphodiesterase regardless of the source of calmodulin (e.g. fat, brain, heart, erythrocytes). LMW appears to be lipid in nature with a molecular weight of 1,500–5,000. The role of these inhibitors in diabetes and mechanism of action of insulin is presented.