Ratha B K, Ramanujan S N
Acta Biochim Biophys Hung. 1986;21(4):381-90.
Specific staining on polyacrylamide gel of acetylcholinesterase (AchE) from brain and muscle of Heteropneustes fossilis showed one major tissue specific band in each. Eserine inhibited the enzyme competitively in both tissue homogenates. However, the normal level of activity and the pattern of the rate of inhibition with increasing eserine concentrations were different. Muscle showed higher AchE specific activity than brain. There was a hyperbolic increase in the percent of inhibition of AchE activity by eserine in muscle whereas in brain the pattern was biphasic. The apparent Km and Vmax in the two tissue homogenates were also different. The results suggest structural and functional variations of AchE in brain and muscle of H. fossilis.
对印度囊鳃鲶的脑和肌肉中的乙酰胆碱酯酶（AchE）在聚丙烯酰胺凝胶上进行的特异性染色显示，每个组织中均有一条主要的组织特异性条带。毒扁豆碱在两种组织匀浆中均竞争性抑制该酶。然而，正常活性水平以及随着毒扁豆碱浓度增加抑制率的模式有所不同。肌肉显示出比脑更高的AchE比活性。毒扁豆碱对肌肉中AchE活性的抑制百分比呈双曲线增加，而在脑中模式是双相的。两种组织匀浆中的表观Km和Vmax也不同。结果表明印度囊鳃鲶脑和肌肉中AchE的结构和功能存在差异。
