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KMID : 0545120130230040467
Journal of Microbiology and Biotechnology
2013 Volume.23 No. 4 p.467 ~ p.472
Glutamine-Induced Production and Secretion of Helicobacter pylori ¥ã-Glutamyltranspeptidase at Low pH and Its Putative Role in Glutathione Transport
Ki Mi-Ran

Yun Na-Rae
Hwang Se-Young
Abstract
Helicobacter pylori increased the ¥ã-glutamyltranspeptidase (GGT) production under low-pH (maximal at pH 4) and appropriate pCO2 conditions, while the production of GGT mRNA correlated with increased total enzyme activity. At pH 4, the bacterium augmented enzyme production in the presence of glutamine (~10 mM) in the medium, which predominantly occurred after a 6-min time-lag. Monovalent salts such as NaCl or NH4Cl facilitated enzymatic activation in acidic solutions of approximately pH 4.5. In addition, glutathione¡¯s ¥ã-glutamyl moiety cysteinylglycine appeared to be taken up readily by the intact H. pylori, but not by the one pretreated with a potent GGT inhibitor, acivicin, suggesting that the GGT may partake in glutathione uptake by the cell.
KEYWORD
Helicobacter pylori, ¥ã-glutamyltranspeptidase, glutamine, glutathione, ammonia
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