Roshchina V V, Aleksandrova I F
Nauchnye Doki Vyss Shkoly Biol Nauki. 1991(12):50-4.
The acetylthiocholine-hydrolyzing enzymatic activity inhibited by the neostigmine and partly physostigmine has been found in extracts from mycelium of fungus Aspergillus niger. The enzyme has been isolated and 15-20 fold purified. The cholinesterase activity of the protein (Kmu 7.10-7 M) is comparable with known for analogous enzymes from higher plants, for its inhibition high concentrations of substrate (greater than 10-3M) are required. The enzyme hydrolyzes acetylthiocholine with rate approximately 1.5 times higher than butyrylthiocholine. Molecular mass of native protein is approximately 600 kDa, subunits -63 and 44 kDa.
在黑曲霉菌丝体提取物中发现了被新斯的明和部分毒扁豆碱抑制的乙酰硫代胆碱水解酶活性。该酶已被分离并纯化了15至20倍。该蛋白质（Km为7.1×10⁻⁷M）的胆碱酯酶活性与高等植物中类似酶的已知活性相当，因为其抑制作用需要高浓度的底物（大于10⁻³M）。该酶水解乙酰硫代胆碱的速率比丁酰硫代胆碱高约1.5倍。天然蛋白质的分子量约为600 kDa，亚基分子量分别为63 kDa和44 kDa。
