Purification and Partial Properties of Recombinant Buckwheat Trypsin Inhibitor

摘要

Recombinant buckwheat trypsin inhibitor(rBTI)was purified by Ni2+-NTA affinity chromatography and Superdex G-75 10/30 HR gel chromatography. The analysis of some properties showed that the bound His6-tagged fusion protein is similar to the native trypsin inhibitors in buckwheat seeds. Its molecular weight is 9 322．1 Da determined by massspectrum analysis. The protein possesses thermostability in tlle pH range 3．0-8．0, after 120 min by heating(100℃)treatment, the inhibitor remained over 70%of its trypsin inhibitory activity．rBTI has a strong inhibition against trypsin and themole ratio was about 1:1．5．