Lissi E A, Clavero N
Departamento de Química, Facultad de Ciencias, Universidad de Santiago, Chile.
Free Radic Res Commun. 1990;10(3):177-84. doi: 10.3109/10715769009149886.
Thermolysis of 2,2'-azo-bis-(2-amidinopropane) under air in the presence of lysozyme leads to extensive inactivation of the enzyme. The number of inactivated enzyme molecules per radical produced increases with the enzyme concentration up to values considerably larger than one. Enzyme inactivation is accompanied by extensive tryptophan modification. Over the enzyme concentration range considered (1.7 to 130 microM) nearly 4 tryptophan groups are modified per enzyme molecule inactivated. Both the inactivation and tryptophan modification are prevented by micromolar concentrations of propyl gallate. The results are interpreted in terms of an efficient inactivation of the enzyme by the alkylperoxyl radicals generated by thermolysis of the azocompound.
在空气中，于溶菌酶存在的情况下对2,2'-偶氮-双-(2-脒基丙烷)进行热解，会导致该酶大量失活。每个产生的自由基所导致的失活酶分子数量会随着酶浓度的增加而增加，直至达到远大于1的值。酶失活伴随着色氨酸的大量修饰。在所考虑的酶浓度范围内（1.7至130微摩尔），每失活一个酶分子，近4个色氨酸基团会被修饰。微摩尔浓度的没食子酸丙酯可防止失活和色氨酸修饰。这些结果可根据由偶氮化合物热解产生的烷基过氧自由基对酶的有效失活来解释。
