Peptide bond scission of staphylococcal enterotoxin C2 and related factors.
- Author:
Yue-Bin YING
1
;
Hong-Ying SUN
;
Ding DING
;
Dan-Xi LI
;
Qiao XUE
;
Shu-Qing CHEN
Author Information
- Publication Type:Journal Article
- MeSH: Amino Acid Sequence; Enterotoxins; chemistry; genetics; Molecular Sequence Data; Protein Conformation; Protein Stability; Recombinant Fusion Proteins; chemistry; genetics
- From: Journal of Zhejiang University. Medical sciences 2009;38(5):505-510
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo investigate the limited digestion of recombinant staphylococcal enterotoxin C2 (SEC2-His)in different conditions.
METHODSThe purified recombinant SEC2-His was treated with different reagents and the cleavage of rSEC2 molecule was observed by SDS-PAGE.
RESULTThe cleavage occurred in positions Cys93-Cys110 of the disulfide loop. Complete auto-cleavage of recombinant SEC2 was observed in solution at 37degrees within 24 hrs, and that was accelerated under alkaline conditions. The auto-cleavage of the recombinant protein was inhibited in the presence of beta-ME (2%), PMSF (5-10 mmol/L), imidazole (1 mol/L) or crude E.coli lysate. Non-specific degradation of recombinant SEC2 was promoted with the increasing of the concentration of H(2)O(2).
CONCLUSIONThe recombinant SEC2-His is broken down in special site of protein, which may be associated with the protein structure.
