期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 89, 期 1, 页码 16-24出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2013.02.002
关键词
Cloning; Expression; pTWIN1; Trypsin sepharose; Chitin beads
类别
资金
- Senior Research Fellowship from Council of Scientific and Industrial Research (CSIR), New Delhi, India
- [MLP-0087]
The seeds of the legume horsegram (Dolichos biflorus), a protein rich pulse (bean), contain multiple forms of Bowman-Birk inhibitors (protease inhibitors). The major inhibitor HGI-III contains seven interweaving disulfides and is extremely stable to high temperatures. A soluble HGI-III (rHGI) with the native N-terminus was produced using a pTWIN IMPACT (TM) purification system. Yield of rHGI was improved by introducing a trypsin sepharose affinity chromatography step resulting in similar to 670 fold purification. The biochemical characteristics of rHGI point to its close similarity to seed HGI-III not only in its structure but also in its inhibitory characteristics toward bovine trypsin and chymotrypsin. The expression and purification strategy presented here promises to produce BBIs in their natural form for pharmacological and therapeutic use. (C) 2013 Elsevier Inc. All rights reserved.
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