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- Title
Heterologous expression, purification, and properties of a chymotrypsin inhibitor isolated from potatoes.
- Authors
Parfenov, I.; Revina, T.; Gerasimova, N.; Kladnitskaya, G.; Valueva, T.
- Abstract
The PKPIJ-B gene encoding a chymotrypsin inhibitor from a subfamily of potato Kunitz-type proteinase inhibitors (PKPI) in potatoes ( Solanum tuberosum L. cv. Yubilei Zhukova) was cloned into a pET23a vector and then expressed in Escherichia coli. The recombinant PKPIJ-B protein obtained in the inclusion bodies was denatured, purified by high-performance liquid chromatography (HPLC) on Mono Q under denaturing conditions, and renaturated. The renaturated protein was additionally purified using HPLC on DEAE-ToyoPearl. The PKPIJ-B protein efficiently suppressed chymotrypsin activity, had a weaker effect on trypsin, and inhibited the growth and development of phytopathogenic microorganisms affecting potato plants.
- Subjects
CHYMOTRYPSIN; POTATOES; ESCHERICHIA coli; MICROORGANISMS; PLANT growth; MICROBIAL herbicides; PLANT diseases
- Publication
Applied Biochemistry & Microbiology, 2013, Vol 49, Issue 1, p28
- ISSN
0003-6838
- Publication type
Article
- DOI
10.1134/S0003683813010146