Stepuro I I, Artsukevich A N, Ostrovskiĭ Iu M
Biofizika. 1981 Sep-Oct;26(5):777-81.
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.
牛血清白蛋白和人血清白蛋白中一个（最不稳定的）二硫键的快速光解分别是由212和214色氨酸残基的敏化作用导致的，它们实际上与二硫键同时分解。在6-8 M胍中未观察到这种效应。在用紫外线通过NaBH4断裂白蛋白二硫键后，观察到蛋白质球状体的构象重排，同时暴露的精氨酸残基减少，而暴露的赖氨酸残基未发生变化。由于精氨酸残基不再暴露于发色团，二硫键还原后1,8-苯胺基萘磺酸盐（ANS）荧光强度降低了60-70%。
