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苦荞类胰蛋白酶水解酶的纯化及部分性质研究
引用本文:李玉英,赵卓慧,杨斌,王转花.苦荞类胰蛋白酶水解酶的纯化及部分性质研究[J].山西大学学报(自然科学版),2003,26(2):173-175.
作者姓名:李玉英  赵卓慧  杨斌  王转花
作者单位:1. 山西大学生命科学与技术学院,山西,太原,030006
2. 南开大学生命科学院,天津,300071
基金项目:山西省科技厅攻关项目 ( 0 110 0 1)
摘    要:采用缓冲液提取、盐析、凝胶过滤及离子交换层析等方法,从苦荞种子中分离纯化出1种类胰蛋白酶水解酶,经十二烷基硫酸钠一聚丙烯酰胺凝胶电泳(SDS—PAGE)测得其分于量为67kD,等电聚焦(IEF)测得等电点为6.3.该酶可以水解胰蛋白酶的底物BApNA,而且其活性不受苦荞胰蛋白酶抑制剂的影响.通过比较,苦荞中的胰蛋白酶水解酶在性质上与报道的甜荞BAPAase极为相似,可能属于同一类蛋白酶.

关 键 词:苦荞  类胰蛋白酶  水解酶  酶活性  纯化  SDS-PAGE  等电聚焦  离子交换层析
文章编号:0253-2395(2003)02-0173-03
修稿时间:2002年9月26日

Isolation and Some Properties of the Trypsin-Like Protease from Tartary Buckwheat Seeds
LI Yu-ying ,ZHAO Zhuo-hui ,YANG Bin ,WANG Zhuan-hua.Isolation and Some Properties of the Trypsin-Like Protease from Tartary Buckwheat Seeds[J].Journal of Shanxi University (Natural Science Edition),2003,26(2):173-175.
Authors:LI Yu-ying  ZHAO Zhuo-hui  YANG Bin  WANG Zhuan-hua
Institution:LI Yu-ying 1,ZHAO Zhuo-hui 1,YANG Bin 2,WANG Zhuan-hua 1
Abstract:A trypsin-like protease from tartary buckwheat seeds was isolated and purified by using buffer extracting, salting out, gel filtration and ion exchange chromatography. It appeared as a single band of about 67 000 dalton on sodium dodecyl sulphate-polyacrylamide gel electrophoresis( SDS-PAGE). The isoelectric focusing (IEF) showed that its isoelectric point (pI) was about 6.3. In addition, it could hydrolyze BApNA( N-benzoyl-D,L-arginine p-nitroanilide), which was the substance of trypsin protease and the hydrolyzing activity was not affected by TBTI (Tartary Buckwheat Trypsin Inhibitor). This property much resembled with that of the reported BAPAase from common buckwheat, which indicated that they might belong to the same kind of protease in plant.
Keywords:Tartary Buckwheat  trypsin-like protease  purification
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