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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

García-Alfonso C, Martínez-Galisteo E, Llobell A, Bárcena J A, López-Barea J

Departamento de Bioquímica y Biología Molecular, Facultad de Veterinaria, Universidad de Córdoba, Spain.

Int J Biochem. 1993 Apr;25(4):513-20. doi: 10.1016/0020-711x(93)90658-2.

The enzyme was rapidly inactivated by NAD(P)H, GSH, dithionite or borohydride, while activity increased in the presence of NAD(P)+ or GSSG. NADH was more efficient for inactivation than NADPH. Redox inactivation required neutral or alkaline pH, was maximal at pH 8.5, and depended on the presence of metal cations. 2. GSSG and dithiothreitol fully protected the enzyme from inactivation at concentrations stoichiometric with NAD(P)H. Ten-fold higher ferricyanide or GSH concentrations were required to obtain partial protection. NAD+ or NADP+ were quite ineffective. 3. GSSG fully reactivated the inactive enzyme at 38 degrees C and neutral to acidic pH (5.5-7.5). Reactivation by dithiothreitol was accomplished in short periods of time at pH 8.5 although the activity was progressively lost afterwards. Ferricyanide and GSH also reactivated the enzyme to different extents.

该酶可被NAD(P)H、谷胱甘肽（GSH）、连二亚硫酸盐或硼氢化物迅速失活，而在NAD(P)+或氧化型谷胱甘肽（GSSG）存在时活性增加。NADH比NADPH对失活更有效。氧化还原失活需要中性或碱性pH，在pH 8.5时最大，且依赖于金属阳离子的存在。2. GSSG和二硫苏糖醇在与NAD(P)H化学计量的浓度下能完全保护该酶不被失活。需要十倍于铁氰化物或GSH的浓度才能获得部分保护。NAD+或NADP+相当无效。3. GSSG在38℃及中性至酸性pH（5.5 - 7.5）时能使失活的酶完全重新激活。在pH 8.5时，二硫苏糖醇能在短时间内实现重新激活，尽管之后活性会逐渐丧失。铁氰化物和GSH也能不同程度地使酶重新激活。

García-Alfonso C, Martínez-Galisteo E, Llobell A, Bárcena J A, López-Barea J

Departamento de Bioquímica y Biología Molecular, Facultad de Veterinaria, Universidad de Córdoba, Spain.

Int J Biochem. 1993 Apr;25(4):513-20. doi: 10.1016/0020-711x(93)90658-2.

The enzyme was rapidly inactivated by NAD(P)H, GSH, dithionite or borohydride, while activity increased in the presence of NAD(P)+ or GSSG. NADH was more efficient for inactivation than NADPH. Redox inactivation required neutral or alkaline pH, was maximal at pH 8.5, and depended on the presence of metal cations. 2. GSSG and dithiothreitol fully protected the enzyme from inactivation at concentrations stoichiometric with NAD(P)H. Ten-fold higher ferricyanide or GSH concentrations were required to obtain partial protection. NAD+ or NADP+ were quite ineffective. 3. GSSG fully reactivated the inactive enzyme at 38 degrees C and neutral to acidic pH (5.5-7.5). Reactivation by dithiothreitol was accomplished in short periods of time at pH 8.5 although the activity was progressively lost afterwards. Ferricyanide and GSH also reactivated the enzyme to different extents.

该酶可被NAD(P)H、谷胱甘肽（GSH）、连二亚硫酸盐或硼氢化物迅速失活，而在NAD(P)+或氧化型谷胱甘肽（GSSG）存在时活性增加。NADH比NADPH对失活更有效。氧化还原失活需要中性或碱性pH，在pH 8.5时最大，且依赖于金属阳离子的存在。2. GSSG和二硫苏糖醇在与NAD(P)H化学计量的浓度下能完全保护该酶不被失活。需要十倍于铁氰化物或GSH的浓度才能获得部分保护。NAD+或NADP+相当无效。3. GSSG在38℃及中性至酸性pH（5.5 - 7.5）时能使失活的酶完全重新激活。在pH 8.5时，二硫苏糖醇能在短时间内实现重新激活，尽管之后活性会逐渐丧失。铁氰化物和GSH也能不同程度地使酶重新激活。