[Changes in the secondary and tertiary structure of serum albumin in interactions with ligands of various structures].
High affinity interactions between blood serum albumin and five substances of various chemical structure, exhibiting distinct physiological activity, were accompanied by alterations in the protein tertiary structure, while the albumin secondary structure was involved in conformational transformation after less effective affinity binding.
D004136:Dinitrobenzenes / Q000494:pharmacology; D006801:Humans; D008024:Ligands; D008466:Mechlorethamine / Q000494:pharmacology; D063086:Organothiophosphates / Q000494:pharmacology; D009946:Organothiophosphorus Compounds / Q000494:pharmacology; D011487:Protein Conformation / Q000187:drug effects; D012709:Serum Albumin; D013050:Spectrometry, Fluorescence; D013729:Terpenes / Q000494:pharmacology
D004136:Dinitrobenzenes; D008024:Ligands; D063086:Organothiophosphates; D009946:Organothiophosphorus Compounds; D012709:Serum Albumin; D013729:Terpenes; C035962:etafos; D008466:Mechlorethamine; C004789:dinobuton; C043622:heterofos
Izmeneniia vtorichnoĭ i tretichnoĭ struktury syvorotochnogo al'bumina pri vzaimodeĭstvii s ligandami razlichnogo stroeniia.