Measurements of plasma glutaredoxin and thioredoxin in healthy volunteers and during open-heart surgery

摘要: Abstract Thioredoxin (Trx) and glutaredoxin (Grx) are both multifunctional redox-active proteins. In this study, Grx was identified in human plasma by immunoaffinity purification. The affinity-purified material from displayed a band of 12 kDa identical to recombinant Western blotting its glutathione-dependent reducing activity β-hydroxyethyl disulfide. Competitive enzyme-linked immunosorbent assays (ELISA) showed that levels (mean ± SD) Trx healthy volunteers (n = 41) were 456 284 ng/ml 28.5 12.6 ng/ml, respectively. cardiac surgical patients 17), did not significantly change during cardiopulmonary bypass (CPB). contrast, arterial measured sandwich ELISA corrected for hemolysis elevated reperfusion the postcardioplegic heart (p .0001 at maximum), whereas competitive increased preparation CPB, but decreased CPB. When oxidized, immunoreactive changed ELISA. These results suggest oxidized is released into There no significant difference between intracoronarial samples, indicating specific release heart. may be important components defense against oxidative stress.