[Changes in serum albumin conformation following exposure to ultraviolet radiation].
Rapid photolysis of one (the most labile) disulfide bridge in bovine and human serum albumines resulted from the sensitizing action of 212 and 214 tryptophane residues, correspondingly, decomposing practically simultaneously with the disulfide bond. This effect was not observed in 6-8 M guanidine. Conformational rearrangement of the protein globule accompanied by a decrease of the exposed arginine residues was observed after the break of the albumine disulfide bond on NaBH4 by ultraviolet, the exposed lisine residues being unaltered. The intensity of 1,8-anilinonaphtalenosulfonate (ANS) fluorescence decreased by 60-70% after the reduction of the disulfide bond due to the arginine residues being unexposed for the chromophore.
D000818:Animals; D002417:Cattle; D006801:Humans; D010782:Photolysis; D011487:Protein Conformation / Q000528:radiation effects; D012709:Serum Albumin / Q000528:radiation effects*; D012710:Serum Albumin, Bovine / Q000528:radiation effects; D013056:Spectrophotometry, Ultraviolet; D014466:Ultraviolet Rays
D012709:Serum Albumin; D012710:Serum Albumin, Bovine
Izmenenie konformatsii syvorotochnykh al'buminov pod deĭstviem ul'trafioletovogo izlucheniiu.