Gorodinskiĭ A I, Dambinova S A
Biull Eksp Biol Med. 1986 Sep;102(9):285-8.
The endogenous factor that inhibited 3H-L-glutamate specific binding (FIB) was isolated from the aqueous extract of the crude mitochondrial fraction of the rat cerebral cortex homogenate and partially purified. The purification procedure involved several steps of ion-exchange, gel-permeating and thin-layer chromatography. Partially purified FIB competitively inhibited 3H-L-glutamate specific binding and had the molecular weight of 450-600 Da. Glutamic acid residues were found in FIB amino acids. The functional role of the isolated factor as an endogenous modulator involved in the regulation of effective synaptic transmission of glutamatergic brain synapses is discussed.
从大鼠大脑皮层匀浆粗线粒体部分的水提取物中分离出抑制3H-L-谷氨酸特异性结合（FIB）的内源性因子，并进行了部分纯化。纯化过程包括离子交换、凝胶渗透和薄层色谱等几个步骤。部分纯化的FIB竞争性抑制3H-L-谷氨酸特异性结合，分子量为450-600 Da。在FIB氨基酸中发现了谷氨酸残基。讨论了分离因子作为内源性调节剂在调节谷氨酸能脑突触有效突触传递中的功能作用。
