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桑尺蠖多酚氧化酶的分离纯化
引用本文:张永亮,朱勇.桑尺蠖多酚氧化酶的分离纯化[J].河南农业科学,2010(5).
作者姓名:张永亮  朱勇
作者单位:1. 周口师范学院,生命科学系,河南,周口,466001
2. 西南大学,生物技术学院,重庆,400715
基金项目:教育部高等学校博士学科点专项科研基金,重庆市教委科学基金 
摘    要:多酚氧化酶是昆虫初生新表皮硬化过程中的关键酶。为了研究桑尺蠖(Phthonandria atrineata)多酚氧化酶的功能与性质,探讨了桑尺蠖多酚氧化酶的分离纯化方法。以桑尺蠖五龄幼虫为材料,用磷酸盐缓冲液提取多酚氧化酶粗提液,再经80%饱和度硫酸铵沉淀、透析及SephadexG-100凝胶过滤进一步分离纯化,得到了部分纯化的多酚氧化酶,其酶纯化倍数为6.28倍,酶得率为3.34%,酶比活力为812.8 U/mg。

关 键 词:桑尺蠖  多酚氧化酶  纯化

Purification of Polyphenol Oxidase from Phthonandria atrineata
ZHANG Yong-liang,ZHU Yong.Purification of Polyphenol Oxidase from Phthonandria atrineata[J].Journal of Henan Agricultural Sciences,2010(5).
Authors:ZHANG Yong-liang  ZHU Yong
Abstract:Polyphenol oxidase is a key enzyme involved in the sclerotization of new cuticular layer of insect.In order to study the function and characters of polyphenol oxidase from the wild silkworm Phthonandria atrineata,isolation and purification methods of polyphenol oxidase from Phthonandria atrineata were explored.Crude polyphenol oxidase was extracted from the 5th instar larvae with sodium phosphate extraction buffer.Partially purified polyphenol oxidase was obtained through 80% saturated(NH4)2SO4,precipitation dialysis,and Sephadex G-100 gel filtration from the crude enzyme.This protocol had a purification factor of 6.28,yield factor of 3.34%,and enzyme specific activity of 812.81U/mg.
Keywords:Phthonandria atrineata  Polyphenol oxidase  Purification
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