PubMed · 1975898
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1990-09-22. Boarding the train.. https://pubmed.ncbi.nlm.nih.gov/1975898/
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Human serum albumin (HSA) is one of the main proteins involved in the binding of drugs and small solutes in blood or serum. This study examined the changes in chromatographic properties that occur for immobilized HSA following the chemical modification of HSA's lone tryptophan residue (Trp-214). Trp-214 was reacted with o-nitrophenylsulfenyl chloride, followed by immobilization of the modified protein and normal HSA onto separate silica-based HPLC supports. The binding properties of the modified and normal HSA were then analyzed and compared by using frontal analysis and zonal elution experiments employing R/S-warfarin and L-tryptophan as probe compounds for the warfarin and indole binding regions of HSA. The modified HSA was found to have the same number of binding sites as normal HSA for R-warfarin and L-tryptophan but lower association equilibrium constants for these test solutes. Zonal elution studies with R- and S-warfarin on the modified HSA column demonstrated the importance of Trp-214 in determining the stereoselective binding of HSA for these agents. These studies also indicated that tryptophan modification can alter HSA-based separations for chiral solutes.
Red blood cell lysis, photosensitized by the products of the aerobic photolysis of benzydamine (1) and azapropazone (4), was investigated. Irradiation of a methanol solution of 1 and 4 under oxygen produces the photoproducts 3-hydroxy-benzydamine, (2), 2-(3-dimethylaminopropyl)-1-benzylindazolin-3-one (3) and 3-dimethylamino-7-methyl-1,2,4-benzotriazine (5). The mechanism of the photodegradation of 1 was examined. Photoproducts 3 and 5 produce singlet oxygen as demonstrated by trapping with 2,5-dimethylfuran. The photohemolysis rate for the photoproducts 3 and 5 was enhanced by deuterium oxide and oxygen. No change was observed in the presence of reduced glutathione. The photohemolysis rate was low under anaerobic conditions.
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