Purification and characters of a novel proteinase A inhibitor from potato tuber
A novel proteinase A inhibitor was purified from potato juice by three successive steps: ammonium sulfate, Sephadex G-50 filtration and CM chromatography. Parts of its characters were analyzed. The results showed that the inhibitor had one subunit with relative molecular weight 16.71 Kda. Its optimum pH limit of inhibition was pH 5 ～5.5, the optimum reaction time 1.5 hour, This inhibitor showed a remarkable heat stability. By investigating the interaction between this inhibitor and a variety of proteinases, it is indicated that the inhibitor was more specific against trpsin and yeast proteinase A than other proteinases. The dissociation constants (Ki) were 2.7 |ì mol/L, and the inhibition type was the complex of non-competitive and competitive inhibition.
proteinase A inhibitor purification potato
Quan LI Yaping Tian
The Key Laboratory of Industrial Biotechnology ，Ministry of Education ，Jiangnan University, Wuxi, 214122, China
国际会议
The 5th International Conference on Separation Science and Technology(第五届国际分离科学与技术会议)
北京
英文
2007-10-14（万方平台首次上网日期，不代表论文的发表时间）