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马铃薯蛋白酶A抑制剂的纯化与性质
引用本文:李泉,田亚平.马铃薯蛋白酶A抑制剂的纯化与性质[J].天然产物研究与开发,2008,20(6).
作者姓名:李泉  田亚平
作者单位:江南大学工业生物技术教育部重点实验室,无锡,214122
摘    要:采用硫酸铵沉淀、Sephadex G-50和CM柱层析,从马铃薯汁中纯化蛋白酶A(protease A,PrA)抑制剂,并对其部分性质进行研究。蛋白酶A抑制剂为单亚基,相对分子质量为16.71kDa。热稳定性良好,抑制最佳pH范围为5—5.5,最佳反应时间为1.5h,对PrA抑制类型为竞争和非竞争性混合抑制作用。

关 键 词:蛋白酶A  抑制剂  分离纯化

Purification and Characters of Protease A Inhibitor from Potato
LI Quan,TIAN Ya-ping.Purification and Characters of Protease A Inhibitor from Potato[J].Natural Product Research and Development,2008,20(6).
Authors:LI Quan  TIAN Ya-ping
Institution:LI Quan,TIAN Ya-ping*The Key Laboratory of Industrial Biotechnology,Ministry of Education,Jiangnan University,Wuxi 214122,China
Abstract:Protease A inhibitor was purified from potato juice by ammonium sulfate,Sephadex G-50 filtration and CM chromatography.Parts of its characters were analyzed.The results showed that the inhibitor had one subunit,and its relative molecular quality was 16.71 kDa.The inhibitor had a good stability,the best pH limit of inhibition was 5-5.5,the best reaction time was 1.5 h,and the inhibition type was the complex of non-competitive and competitive inhibition.
Keywords:A
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