Terato H, Yamamoto O
Division of Gene Chemistry, Graduate School of Gene Science, Faculty of Sciences, Hiroshima University, Japan.
Biochem Mol Biol Int. 1994 Sep;34(2):295-300.
Tyrosinase (0.2 mg/ml of 0.1 M phosphate buffer solution, pH 6.5) which has cresolase and catecholase activities was irradiated with 60Co gamma-rays. The cresolase activity was measured at varying radiation doses under various atmospheric conditions. D0 was found to be 350 Gy in N2-saturated solution. The OH radical has been shown to be the main species involved in radiation-induced enzyme inactivation. However, in this study, OH radical scavengers, t-BuOH and MeOH, had no effect. O2 which acts generally as an enhancer of OH-induced enzyme inactivation also had little effect, but N20 ae aq scavenger, and Cu++ markedly inhibited the inactivation indicating that e aq is the main species involved in inactivating the cresolase activity, reducing Cu++ as the active center.
将具有甲酚酶和儿茶酚酶活性的酪氨酸酶(0.2毫克/毫升的0.1M磷酸盐缓冲溶液,pH值6.5)用60Coγ射线辐照。在各种大气条件下,于不同辐射剂量下测定甲酚酶活性。在氮气饱和溶液中,D0值为350戈瑞。已证明羟基自由基是辐射诱导酶失活的主要相关物质。然而,在本研究中,羟基自由基清除剂叔丁醇和甲醇没有效果。通常作为羟基诱导酶失活增强剂的氧气也几乎没有影响,但N2O作为水合电子清除剂,以及Cu++显著抑制失活,表明水合电子是使甲酚酶活性失活的主要相关物质,它将作为活性中心的Cu++还原。