Hypochlorite-induced damage of plasminogen molecules: structural-functional disturbance

Abstract

Plasminogen being a precursor of plasmin, a serine protease which plays a fundamental role in the intravascular thrombolysis. For the first time, by using high-resolution mass spectrometry, data were obtained of oxidative modifications of the plasminogen molecule under induced oxidation. The FTIR data show that under oxidation on the protein, its secondary structure also undergoes the rearrangements. The high tolerance of plasminogen to oxidation can be due to both the closed conformation and the ability of some Met residues to serve as ROS trap.