Tometsko A M, Turula J
Int J Pept Protein Res. 1976;8(3):331-6. doi: 10.1111/j.1399-3011.1976.tb02511.x.
The photosensitive inactivation of trypsin and chymotrypsin by 4-fluoro-3-nitrophenyl azide (FNPA) is described. A dark inhibition was observed at elevated probe concentrations, and was reversible. The enzymes were stable to photolysis in the absence of probe. Photolytic inactivation of trypsin and chymotrypsin with FNPA was found to be irreversible, and occurs in minutes at concentrations of FNPA where dark inhibition is negligible. The photoprobe was equally effective at pH 3 or pH 8. Nonspecific inactivation appears to be low, as evidenced by the stability of glucose oxidase and peroxidase to photolysis with FNPA.
描述了4-氟-3-硝基苯叠氮化物（FNPA）对胰蛋白酶和胰凝乳蛋白酶的光敏失活作用。在探针浓度升高时观察到暗抑制，且该抑制是可逆的。在没有探针的情况下，酶对光解稳定。发现用FNPA对胰蛋白酶和胰凝乳蛋白酶进行光解失活是不可逆的，并且在暗抑制可忽略不计的FNPA浓度下，几分钟内即可发生。该光探针在pH 3或pH 8时同样有效。葡萄糖氧化酶和过氧化物酶对FNPA光解的稳定性证明非特异性失活似乎较低。
