Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5167395 | Phytochemistry | 2007 | 9 Pages |
Abstract
A sucrose binding protein from soybean, which contains two conserved barrel domains (1) of the cupin superfamily, was bacterially produced, affinity-purified, renatured and characterized. The refolded his-tagged protein regained its sucrose binding capacity and it was highly thermo and chemical stable, suggesting it was properly folded into a bicupin structure.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Carolina S. Rocha, Dirce F. Luz, Marli L. Oliveira, Maria C. Baracat-Pereira, Francisco Javier Medrano, Elizabeth P.B. Fontes,