Gazzotti P, Gloor M, Carafoli E
Biochem Biophys Res Commun. 1984 Feb 29;119(1):343-51. doi: 10.1016/0006-291x(84)91657-7.
Calmodulin binding proteins have been found in submitochondrial fractions obtained from highly purified rat liver mitochondria. The matrix fraction contains two major calmodulin binding proteins: one, having Mr of 145,000, apparently is carbamoyl-phosphate synthetase. Another has a Mr of 58,000 and has not been associated with enzyme activities. A major calmodulin binding protein of unknown function and having Mr of 32,000 has been found in the Triton X-100 solubilizate of the inner membrane. Minor amounts of two calmodulin binding proteins having Mr of about 37,000 and 56,000 have been found in the outer membrane.
在从高度纯化的大鼠肝脏线粒体获得的亚线粒体组分中发现了钙调蛋白结合蛋白。基质组分含有两种主要的钙调蛋白结合蛋白:一种分子量为145,000,显然是氨甲酰磷酸合成酶。另一种分子量为58,000,且与酶活性无关。在内膜的Triton X-100增溶物中发现了一种功能未知、分子量为32,000的主要钙调蛋白结合蛋白。在外膜中发现了少量分子量约为37,000和56,000的两种钙调蛋白结合蛋白。