Brief Reports
Copyright ©The Author(s) 2003. Published by Baishideng Publishing Group Inc. All rights reserved.
World J Gastroenterol. May 15, 2003; 9(5): 1119-1122
Published online May 15, 2003. doi: 10.3748/wjg.v9.i5.1119
Recombinant Helicobacter pylori catalase
Yang Bai, Ya-Li Zhang, Jian-Feng Jin, Ji-De Wang, Zhao-Shan Zhang, Dian-Yuan Zhou
Yang Bai, Ya-Li Zhang, Ji-De Wang, Dian-Yuan Zhou, PLA Institute for Digestive Medicine, Nanfang Hospital, the First Military Medical University, Guangzhou 510515, Guangdong Province, China
Jian-Feng Jin, Chemistry university of Beijing, Beijing 100071, China
Zhao-Shan Zhang, Institute of Biotechnology, Chinese Academy of Military Medical Sciences, Beijing 100071, China
Author contributions: All authors contributed equally to the work.
Supported by the National Natural Science Foundation of China, No. 30270078
Correspondence to: Dr Yang Bai, PLA Institute for Digestive Medicine, Nanfang Hospital, the First Military Medical University, Guangzhou 510515, Guangdong Province, China. baiyang1030@hotmail.com
Telephone: +86-20-61641532
Received: November 6, 2002
Revised: November 23, 2002
Accepted: December 7, 2002
Published online: May 15, 2003
Abstract

AIM: To construct a recombinant strain which highly expresses catalase of Helicobacter pylori (H. pylori) and assay the activity of H. pylori catalase.

METHODS: The catalase DNA was amplified from H. pylori chromosomal DNA with PCR techniques and inserted into the prokaryotie expression vector pET-22b (+), and then was transformed into the BL21 (DE3) E. coli strain which expressed catalase recombinant protein. The activity of H. pylori catalase was assayed by the Beers&Sizers.

RESULTS: DNA sequence analysis showed that the sequence of catalase DNA was the same as GenBank’s research. The catalase recombinant protein amounted to 24.4% of the total bacterial protein after induced with IPTG for 3 hours at 37 °C and the activity of H. pylori catalase was high in the BL21 (DE3) E. coli strain.

CONCLUSION: A clone expressing high activity H. pylori catalase is obtained, laying a good foundation for further studies.

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