Fluck R A, Jaffe M J
Biochim Biophys Acta. 1975 Nov 20;410(1):130-4. doi: 10.1016/0005-2744(75)90213-2.
Enzymes capable of hydrolyzing esters of thiocholine have been assayed in extracts of Solanum melongena L. (eggplant) and Zea Mays L. (corn). The enzymes from both species are inhibited by the anti-cholinesterases neostigmine, physostigmine, and 284c51 and by AMO-1618, a plant growth retardant and they both have pH optima near pH 8.0. The enzyme from eggplant is maximally active at a substrate concentration of 0.15 mM acetylthiocholine and is inhibited at higher substrate concentrations. On the basis of this last property, the magnitude of inhibition by the various inhibitors, and the substrate specificity, we conclude that the enzyme from eggplant, but not that from corn, is a cholinesterase.
已对茄属植物（茄子）和玉米（玉米）提取物中能够水解硫代胆碱酯的酶进行了测定。这两个物种的酶都受到抗胆碱酯酶新斯的明、毒扁豆碱和284c51以及植物生长抑制剂AMO - 1618的抑制，并且它们的最适pH值都接近8.0。茄子中的酶在底物浓度为0.15 mM乙酰硫代胆碱时活性最高，在较高底物浓度下受到抑制。基于这一特性、各种抑制剂的抑制程度以及底物特异性，我们得出结论，茄子中的酶是一种胆碱酯酶，而玉米中的酶不是。
