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. 1999 Jul 1;190(1):135–140. doi: 10.1084/jem.190.1.135

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© 1999 The Rockefeller University Press

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Immunoprecipitation of nitrated proteins and PGI₂ synthase in hypoxia-reoxygenated BCA. (A) Proteins from normal or hypoxia-reoxygenated BCA were immunoprecipitated with a polyclonal Ab against PGI₂ synthase (α-PGI₂ synthase) after hypoxia–reoxygenation. As described in Materials and Methods, proteins precipitated by α-PGI₂ synthase were separated electrophoretically and immunostained with a monoclonal α-PGI₂ synthase (left) or a monoclonal α-nitrotyrosine (right). Lane A, hypoxia–reoxygenation + L-NMMA; lane B, hypoxia–reoxygenation + SOD; lane C, hypoxia–reoxygenation; lane D, control. (B) 3-nitrotyrosine–positive proteins were precipitated by an mAb against 3-nitrotyrosine. Proteins were separated similarly and analyzed by immunoblots with polyclonal Ab against PGI₂ synthase. Lane A, control; lane B, hypoxia–reoxygenation; lane C, hypoxia–reoxygenation + L-NMMA; lane D, hypoxia–reoxygenation + SOD.

Immunoprecipitation of nitrated proteins and PGI₂ synthase in hypoxia-reoxygenated BCA. (A) Proteins from normal or hypoxia-reoxygenated BCA were immunoprecipitated with a polyclonal Ab against PGI₂ synthase (α-PGI₂ synthase) after hypoxia–reoxygenation. As described in Materials and Methods, proteins precipitated by α-PGI₂ synthase were separated electrophoretically and immunostained with a monoclonal α-PGI₂ synthase (left) or a monoclonal α-nitrotyrosine (right). Lane A, hypoxia–reoxygenation + L-NMMA; lane B, hypoxia–reoxygenation + SOD; lane C, hypoxia–reoxygenation; lane D, control. (B) 3-nitrotyrosine–positive proteins were precipitated by an mAb against 3-nitrotyrosine. Proteins were separated similarly and analyzed by immunoblots with polyclonal Ab against PGI₂ synthase. Lane A, control; lane B, hypoxia–reoxygenation; lane C, hypoxia–reoxygenation + L-NMMA; lane D, hypoxia–reoxygenation + SOD.