ABSTRACT
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.
