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

doi:10.15625/0866-7160/v25n3.6839

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

Authors

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

DOI: https://doi.org/10.15625/0866-7160/v25n3.6839

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 70^oC 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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Published

02-09-2015

How to Cite

Quang, L. T., Nam, N. P., Ha, P. T., & Tran Chau, P. T. (2015). Purification and some properties of two protein proteinase inhibitors from the seeds of Sophora japonica L. f. Academia Journal of Biology, 25(3), 59–65. https://doi.org/10.15625/0866-7160/v25n3.6839