阿托品对人红细胞中梭曼抑制的乙酰胆碱酯酶老化及重活化的影响。初步报告
Influence of atropine upon ageing and reactivation of soman inhibited acetylcholinesterase from human erythrocytes. Preliminary communication.
作者信息
Kuhnen H, Schrichten A, Schoene K
出版信息
Arzneimittelforschung. 1985;35(9):1454-6.
From human blood concentrates erythrocyte "ghosts" were prepared. These and an enzyme solution, obtained by Triton X 100 treatment of the ghosts, were reacted with 1.2.2-trimethylpropyl-methyl-phosphonylfluoridate (soman). The rate constants of inhibition of the membrane bound and solubilized acetylcholinesterase (AChE) were determined at 3 degrees C, pH 8 and 9 to be 2 X 10(7) and 1.4 X 10(7) mol-1 min-1, respectively. Ageing of the phosphonylated AChE occurred with rate constants of 3.5 X 10(-2) (ghost bound) and 1.3 X 10(-2) (solubilized) min-1 at 3 degrees C, pH 8. 5 X 10(-4) mol/l atropine decreased the ageing rate by 50%. Reactivation of the non aged phosphonyl-AChE by several pyridinium oximes was enhanced by atropine with the ghost-bound enzyme; the reactivation of the phosphonylated solubilized enzyme, however, was not affected by atropine.
从人血浓缩物中制备了红细胞“血影”。将这些血影以及通过用 Triton X 100 处理血影获得的酶溶液与 1.2.2 - 三甲基丙基 - 甲基 - 磷酰氟化物（梭曼）反应。在 3℃、pH 8 和 9 条件下测定膜结合型和可溶型乙酰胆碱酯酶（AChE）的抑制速率常数分别为 2×10⁷ 和 1.4×10⁷ mol⁻¹ min⁻¹。在 3℃、pH 8 条件下，磷酰化 AChE 的老化速率常数分别为 3.5×10⁻²（血影结合型）和 1.3×10⁻²（可溶型）min⁻¹。5×10⁻⁴ mol/L 的阿托品可使老化速率降低 50%。几种吡啶肟对未老化的磷酰化 AChE 的重活化作用在血影结合型酶中因阿托品而增强；然而，磷酰化可溶型酶的重活化不受阿托品影响。
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