Hemoglobin Catalytic Hydrogen Peroxide Oxidation Tyrosine Of Hemoglobin Of Protection

Hemoglobin oxygen carriers used in ischemia reperfusion, because ischemia-reperfusion produce of reactive oxygen species (ROS) and activity of nitrogen (RNS) itself to the body damage to the role, then more likely to be reactive oxygen species (ROS) and activity of nitrogen (RNS) oxidation Hb reaction,formed to carry oxygen to lose the function Fe+Hb,are more likely to be reactive oxygen species cluster (ROS) and activity of nitrogen (RNS) oxidation reaction,formed to carry oxygen to lose the function Fe3+Hb, at the same time induce to the generation of reactive oxygen free radical, Hb constantly oxidation prompted Fe3+Hb and Fe4+Hb form vicious circle.Be become to accumulate a large number of oxygen free radicals at the same time,Fe4THb is a strong oxidizer,cause lipid peroxidation, form the lipid free radicals,protein modification and DNA fracture and so on a series of cascade,thus increasing the ischemia-reperfusion injury,so this question needs to be improved.This paper finds that the hemoglobin protein ferrous with special peroxidase activity,can catalytic hydrogen peroxide oxidation tyrosine reaction,In this paper the characteristics of hemoglobin enzymes of the relative validation,the purpose of the research is to use hemoglobin catalytic activity of enzyme.With tyrosine in HBOC to eliminate H2O2oxidation hemoglobin and remove H2O2,to protect the hemoglobin oxygen carriers,to lessen ischemia-reperfusion injury.ResultOf tyrosine with hydrogen donor substrates, through the fluorescence method to detect Hb or PolyHb in Tyr and H2O2reaction system reaction products fluorescence, Verify that Hb have peroxide enzymes characteristics, it catalytic oxidation of H2O2hydrogen donor substrate tyrosine fluorescence reaction, in0.02mol/L pH7.4of PB buffer found Hb or PolyHb have enhanced role to the reaction products the fluorescence intensity,And hemoglobin combined with CO,We found the reaction products fluorescence not enhance. Explain the hemoglobin enzyme catalysis activity in the iron porphyrins ring,so as to prove the hemoglobin has the enzyme catalysis;Based on this through the ultraviolet method to detect the presence of tyrosine in, change of PolyHb or Hb absorption peaks spectra and the change of the Fe4+Hb formation.The results found that the presence of tyrosine,Hb or PolyHb two absorption peaks characteristics have not changed and Fe4+Hb clearly influenced by the inhibition in620nm.The experimental results of the above the conclusion that Hb or HBOC is oxide catalytic effect of mimetic enzyme,main is heme/Fe2+play a part the catalysis,at the same time in the hemoglobin with tyrosine,restrain the oxidation of hemoglobin,so tyrosine of hemoglobin oxygen carriers in ischemia-reperfusion injury which has potential applications,needs to be further study the specific protection mechanism.