Rukhadze Marina D, Dzidziguri Diana V, Giorgobiani Nana M, Kerkenjia Salome M
Laboratory of Neurobiology and Department of Chemistry, Tbilisi State University, I. Chavchavadze Ave 3, Tbilisi 0128, Georgia.
Biomed Chromatogr. 2005 Jan;19(1):36-42. doi: 10.1002/bmc.413.
The protein fraction of the brain of white rat inhibiting the proliferation of homological cells was studied by hydrophobic interaction and reversed-phase liquid chromatography. The hybrid modification of hydrophobic interaction and biopartitional micellar chromatography was also applied for the elution of hydrophobic component of brain protein fraction. It was established that this protein fraction represents a hydrophilic-hydrophobic complex. The binding of pharmacological preparations with the brain protein fraction in the model system was also investigated. The separation of free and protein bound fractions of drugs was carried out by cloud-point extraction. It was shown that the degree of binding of phenobarbital with the mentioned protein fraction exceeds the same values for carbamazepine and chlorpromazine.
通过疏水相互作用和反相液相色谱法研究了抑制同源细胞增殖的白鼠脑蛋白组分。疏水相互作用和生物分配胶束色谱的混合修饰也用于洗脱脑蛋白组分的疏水成分。已确定该蛋白组分代表亲水 - 疏水复合物。还研究了模型系统中药理制剂与脑蛋白组分的结合。通过浊点萃取法分离药物的游离和蛋白结合组分。结果表明，苯巴比妥与上述蛋白组分的结合程度超过卡马西平和氯丙嗪的相同值。
