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[Renaturation of thermolabile hemolysin inclusion bodies expressed by Vibrio parahaemolyticus].
- Source :
-
Di 1 jun yi da xue xue bao = Academic journal of the first medical college of PLA [Di Yi Jun Yi Da Xue Xue Bao] 2004 Sep; Vol. 24 (9), pp. 995-7. - Publication Year :
- 2004
-
Abstract
- Objective: To clone and construct expression vector pET32a+-tlh to acquire biologically functional thermolabile hemolysin of Vibrio parahaemolyticus.<br />Methods: tlh gene was cloned and the expression vector pET32a+-tlh constructed. The tlh gene of Vibrio parahaemolyticus was expressed in DE3 in the form of inclusion body, which was resolved in 8 mol/L urea followed by purification of the fusion protein using affinity chromatography and renaturation through gradient dialysis, protein concentration reduction and oxidoreduction.<br />Results and Conclusion: The purified and renatured protein possessed hemolytic and immunogenic activities.
- Subjects :
- Cloning, Molecular
Hemolysin Proteins genetics
Inclusion Bodies metabolism
Recombinant Fusion Proteins biosynthesis
Recombinant Fusion Proteins genetics
Vibrio parahaemolyticus genetics
Genetic Vectors
Hemolysin Proteins biosynthesis
Protein Renaturation
Vibrio parahaemolyticus metabolism
Subjects
Details
- Language :
- Chinese
- ISSN :
- 1000-2588
- Volume :
- 24
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Di 1 jun yi da xue xue bao = Academic journal of the first medical college of PLA
- Publication Type :
- Academic Journal
- Accession number :
- 15447844