Woscholski R, Marmé D
Institute of Molecular Cell Biology, University of Freiburg, Germany.
Biochem Biophys Res Commun. 1992 Jan 15;182(1):232-7. doi: 10.1016/s0006-291x(05)80135-4.
Rabbit skeletal muscle membranes contain a protein which inhibits the cAMP-dependent protein kinase. The activity of the partially purified membrane protein is characterized by an IC-50 of 10 to 30 nM with respect to the inhibition of the activity of the catalytic subunit of the cAMP-dependent protein kinase and is sensitive to treatment with heat, acid, alkali and trypsin. The active fractions contain proteins ranging from 40 to 120 kDa, analysed by SDS-gel electrophoresis.
兔骨骼肌膜含有一种抑制环磷酸腺苷(cAMP)依赖性蛋白激酶的蛋白质。部分纯化的膜蛋白活性表现为,相对于抑制cAMP依赖性蛋白激酶催化亚基的活性,其半数抑制浓度(IC-50)为10至30纳摩尔,并且对热、酸、碱和胰蛋白酶处理敏感。通过十二烷基硫酸钠-凝胶电泳(SDS-凝胶电泳)分析,活性组分含有分子量范围在40至120千道尔顿的蛋白质。