Purification and some properties of two protein proteinase inhibitors from the seeds of Sophora japonica L. f.

Le Trong Quang, Nguyen Phuong Nam, Phan Thi Ha, Pham Thi Tran Chau

Abstract


Using column chromatography on superdex-75, MonoS and PAGE methods allowed to separate two highly purified protein proteinase inhibitors from Sophora japonica seeds, named SJ-I and SJ-II. Each of them showed inhibitory activity against both trypsin and chymotripsin.

The molecular mass of both inhibitors were estimated around 16 kDa. However, they were different in pI value: 6.2 for SJ-I and 5.85 for SJ-II.

The heat stability of two inhibitors was also similar: after the treatment of inhibitors at 70oC for 3 min, TIA remained 40% and after 15 min, TIA completely lost.

All obtained data led to a suggestion that SJ-I and SJ-II were isoforms and might be a Bowman - Birk type double headed inhibitors of higher molecular mass.


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DOI: https://doi.org/10.15625/0866-7160/v25n3.6839 Display counter: Abstract : 48 views. PDF : 43 views.

 

                 

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