Crynodeb
Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (≥ 30 mg/liter). N-terminal sequence analysis, SDS-PAGE, RP-HPLC, cd spectroscopy, and small angle X-ray scattering demonstrated that their physicochemical properties were similar to those of C hordeins isolated from barley grain. This indicates that the expressed proteins were correctly folded. The cysteine-containing mutant showed evidence of polymer formation in E. coli, nonreduced preparations of the protein showing the presence of polymers that were replaced by a single protein when a reducing agent was added.
Iaith wreiddiol | Saesneg |
---|---|
Tudalennau (o-i) | 357-363 |
Nifer y tudalennau | 7 |
Cyfnodolyn | Protein Expression and Purification |
Cyfrol | 5 |
Rhif cyhoeddi | 4 |
Dynodwyr Gwrthrych Digidol (DOIs) | |
Statws | Cyhoeddwyd - Awst 1994 |
Cyhoeddwyd yn allanol | Ie |