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( Gunam,Ida Bagus Wayan ),( Kenta Yamamura ),( I Nengah Sujaya ),( Nyoman Semadi Antara ),( Wayan Redi Aryanta ),( Michiko Tanaka ),( Fusao Tomita ),( Teruo Sone ),( Kozo Asano ) 한국미생물 · 생명공학회 2013 Journal of microbiology and biotechnology Vol.23 No.4
Helicobacter pylori increased the γ-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 γ-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.