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Epitope for antibodies inhibiting H. pylori urease characterized.
2004 JUL 7 - (NewsRx.com & NewsRx.net) -- Scientists have characterized the epitope for monoclonal antibodies inhibiting enzymatic activity of Helicobacter pylori urease.
"Two characteristic monoclonal antibodies (HpU-2 and -18) out of 26 monoclonal antibodies (HpU-1 (approx)26) produced against Helicobacter pylori urease showed a strong inhibitory effect against the enzymatic activity of the urease. Epitope mapping about some monoclonal antibodies of the HpU-series inhibiting enzymatic activity was performed by using a surface plasmon resonance apparatus and by digesting H. pylori urease with trypsin, followed by mass spectroscopy," researchers in Japan report.
"The sequences of the epitopes recognized by HpU-2 and -18 were SVELIDIGGNRRIFGFNALVDR (22 mer) and IFGFNALVDR (10 mer), respectively," stated Ryoji Fujii and collaborators at Hiroshima Prefectural University and Fukuyama Medical Laboratory Company. "The former sequence is present as a part of a loop structure at a position close to the C-terminal of the alpha-subunit of H. pylori urease, although it has been suggested that the active site of the urease resides in the beta-subunit."
"The above peptide (22 mer) was chemically synthesized in a linear and cyclic form, and its conjugate with BSA was ...
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Source: HighBeam Research, Epitope for antibodies inhibiting H. pylori urease characterized.