A human receptor protein (AhRC?553) has shown suppressive effects on tumor growth in HeLa cells, but the mechanism remains unknown.  To shed light on this mechanism, structural insights are needed.  Reported here is the characterization of disulfide bridge formation in AhRC?553 by gel electrophoresis and AP-MALDI-MS.  This characterization provides information regarding the secondary structure of this protein.AhRC?553 was analyzed by 1-D SDS-PAGE under two conditions (with and without �-mercaptoethanol). When run with �-mercaptoethanol only one dominant band was present on the gel, which matched the molecular weight of AhRC?553 (~33 kDa). The band's identity was confirmed to be AhRC?553 via an in gel digestion and AP-MALDI-MS. When AhRC?553 was run without �-mercaptoethanol two prominent bands were observed at ~33 kDa and ~70 kDa, representing a monomer and dimer of AhRC?553; both were confirmed via AP-MALDI-MS. These results demonstrate the importance of disulfide bridges in AhRC?553 folding.

Characterization of disulfide bridge sites in <i>Escherichia coli</i> expressed AhRC[Delta]553 protein by AP-MALDI-MS

243rd National Meeting (2012)

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Characterization of disulfide bridge sites in Escherichia coli expressed AhRC[Delta]553 protein by AP-MALDI-MS