[Peptide bond scission of staphylococcal enterotoxin C2 and related factors].
To investigate the limited digestion of recombinant staphylococcal enterotoxin C2 (SEC2-His)in different conditions.



The purified recombinant SEC2-His was treated with different reagents and the cleavage of rSEC2 molecule was observed by SDS-PAGE.



The 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).



The recombinant SEC2-His is broken down in special site of protein, which may be associated with the protein structure.
Ying
Yue-Bin
YB
Institute of Pharmacology, Toxicology and Biological Pharmaceutics, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou, 310058, China.
Sun
Hong-Ying
HY
Ding
Ding
D
Li
Dan-Xi
DX
Xue
Qiao
Q
Chen
Shu-Qing
SQ
D000595:Amino Acid Sequence; D004768:Enterotoxins / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D055550:Protein Stability; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics
D004768:Enterotoxins; D011993:Recombinant Fusion Proteins; C034959:enterotoxin C, staphylococcal