Electron paramagnetic resonance spectra of catalase in mammalian tissues.
The relatively small number of paramagnetic species and the high concentration of catalase in mammalian liver and blood make it possible to directly study this enzyme in frozen whole tissue. The EPR spectra of catalase are dependent on the heme environment and in human blood only catalase A, gxy = 6.48, 5.36 is observed whereas in liver a second spectrum, catalase B, gxy = 6.80, 5.07 can also be seen. Using rapid freeze techniques it has been shown that in rat liver catalase A corresponds to the in vivo steady state and that after death this is largely converted into catalase B. Data from the perfusion of rat livers with oxygenated and deoxygenated blood and dextran solutions together with results from in vitro studies of catalase are interpreted as indicating that catalase B results from the interaction of catalase with an organic acid, most probably formic acid, that the acid is a peroxidative substrate for catalase in vivo and that peroxidation of the acid is not the major role for catalase in rat liver. Catalase binding with other small molecules in intact liver has been demonstrated by perfusion with nitrite-containing dextrans and by intraperitoneal injection of 3-amino-1,2,4-triazole.
D000640:Amitrole / Q000494:pharmacology; D000818:Animals; D002374:Catalase / Q000097:blood; D003911:Dextrans; D004578:Electron Spin Resonance Spectroscopy; D004912:Erythrocytes / Q000201:enzymology*; D005615:Freezing; D006801:Humans; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D010477:Perfusion; D011487:Protein Conformation; D051381:Rats
D003911:Dextrans; D002374:Catalase; D000640:Amitrole