Wang H X, Ng T B
Department of Microbiology, China Agricultural University, Beijing, China.
Biochem Biophys Res Commun. 2004 Sep 10;322(1):17-21. doi: 10.1016/j.bbrc.2004.07.075.
A laccase with a novel N-terminal sequence, a molecular mass of 63kDa, and inhibitory activity toward HIV-1 reverse transcriptase (IC(50)=9.5microM) was isolated from dried fruiting bodies of the monkey head mushroom Hericium erinaceum. A chromatographic procedure involving ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose and fast protein liquid chromatography-gel filtration on Superdex 75 was employed. The laccase was adsorbed on DEAE-cellulose and Q-Sepharose but unadsorbed on CM-cellulose. High activity of the enzyme was observed at pH 3-5 and at 50-80 degrees C. Its activity was completely abolished at pH 8 and 9 and after boiling for 10min. A temperature of 50 degrees C and a pH of 5.0 were optimal for its activity.
从猴头菇(Hericium erinaceum)的干燥子实体中分离出一种漆酶,其N端序列新颖,分子量为63kDa,对HIV-1逆转录酶具有抑制活性(IC(50)=9.5微摩尔)。采用了包括在DEAE-纤维素、CM-纤维素和Q-琼脂糖上进行离子交换色谱以及在Superdex 75上进行快速蛋白质液相色谱-凝胶过滤的色谱方法。该漆酶吸附在DEAE-纤维素和Q-琼脂糖上,但不吸附在CM-纤维素上。在pH 3-5和50-80℃时观察到该酶的高活性。在pH 8和9以及煮沸10分钟后,其活性完全丧失。50℃的温度和5.0的pH对其活性最为适宜。