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The interaction between hemoglobin and peroxiredoxin 2 was Proved by Coimmunoprecipitation Coupled with hemoglobin release test、SDS-PAGE and MS

The Interaction between Hemoglobin and Peroxiredoxin 2 was P...

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中国生物化学与分子生物学会第十一次会员代表大会暨201...

作者：安亮李晓晶谢彩霞魏春华杜晓红苏燕包头医学院

In this study,Co-immunoprecipitation was used to study the interactions between hemoglobin(Hb)and other proteins within erythrocytes.First,the fresh normal adult anticoagulatedwhole blood was washed with saline 4-5 times to prepare packed RBCs,whichwere further prepared into erythrocytes suspension and hemolysate respectively.Second,the erythrocytessuspension and hemolysate were electrophoresesed on the starchagarosemixed gel at the same time,and then the bands of HbA,HbA2 and HbA-HbA2 oferythrocyte sample and the corresponding bands of hemolysate sample were cut out fromthe gel.Third,proteins within the gel were enriched by freeze-thaw method,then the proteinsamples were co-immunoprecipitated with hemoglobinβantibody.The immunocomplexeswere then separated by 5–12%SDS-PAGE.7 kind of protein was emerged,and an2 kD protein band emerged in both erythrocytes HbA and hemolysate HbA.Finally,the2 kD band was cut out and analyzed by Q–TOF MS.The MS results showed that thisband was peroxiredoxin 2(Prx-2),an antioxidant enzyme,which uses cysteine residues todecompose peroxides.Prx-2 is the third most abundant protein in erythrocytes,and competeseffectively with catalase and glutathione peroxidase to scavenge low levels of hydrogenperoxide,including that derived from hemoglobin autoxidation.So we can concludethat the special interaction between Hb and peroxiredoxin 2 can help Prx2 defend theautoxidation of hemoglobin within erythrocytes,however,whether the interaction hassome relationship with clinical diseases still needs further research.

关键词： Hemoglobin Peroxiredoxin 2 Interaction Hemoglobin Release Test

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