2007•Hubei nongye kexueRequires access
Study on Parition,Purification and Activity of Acetylcholinesterase in Crucian Muscle
Ying Xu
Open publisher page 0 citations
Abstract
The crucian muscle is employed as raw material to extract AChE.The activity of crude enzyme is determined by means of the colorimetric modified method of Ellman under three different conditions(pH,temperature and time)which are designed with orthogonal matrix.Then the optimal conditions of analyzing the activity of AChE and AChE with high activity is gained.The purification of one enzyme with highest activity is carried on by DEAE-Sephadex A-50 and Sephadex G-200.The results indicate that the effects on the activity of AChE are in the order of temperaturepHtime;the optimal conditions are: pH 8.0,35℃,30 minutes.The purification multiple of DEAE-Sephadex A-50 is 17.73 and the purification multiple of Sephadex G-200 is 47.29.The yield of DEAE-Sephadex A-50 is 40.06 % and the yield of Sephadex G-200 is 20.65%.