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观察了部分纯化的人肝 G类毒剂水解酶 ( G酶 )的一些生化性质 .二硫苏糖醇 ( 5mmol·L-1)使G酶活性在 37℃ ,30 min内抑制 35% ;对氯汞苯甲酸 ( 1 - 1 0 0 0 μmol· L-1)不影响 G酶活性 .说明二硫键对酶分子的三维结构至关重要 ,而没有游离巯基参与酶的催化反应 .人肝 G酶专一性地水解带P- F键的有机磷化合物梭曼 ,但不催化带 P- O,P- C或 P- S键的有机磷化合物的反应 .
Some biochemical properties of partially purified human liver G-type enzyme hydrolase (Gase) were observed. Dithiothreitol (5 mmol·L -1) inhibited G-enzyme activity by 35% at 37 ° C for 30 min; Mercuric benzoate (1-10,000 μmol · L-1) did not affect G-enzyme activity, indicating that the disulfide bond is crucial for the three-dimensional structure of the enzyme molecule and that no free sulfhydryl group participates in the catalytic reaction of the enzyme. The organophosphorus compound Soman with P-F bonds is specifically hydrolyzed, but does not catalyze the reaction of organophosphorus compounds with P-, P-, or P- S bonds.