Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell.
A thiol-dependent antioxidant protein (HRPRP) was previously reported as a predominant antioxidant protein in human red blood cell (RBC). The analysis of amino acid sequence of HRPRP with those of human PRP-like gene products indicates that HRPRP is identical to brain PRP (HPRP). This protein act as a peroxidase linked to thioredoxin (Trx)/thioredoxin reductase (TR). Until now, there was no evidence for Trx/TR system in RBC. The existence of the Trx/TR system in RBC was immunologically determined. A 58-kDa protein showing TR activity was partially purified from human RBC and characterized. Our results reveal that HRPRP act as a new type of peroxidase supported by Trx/TR system in human RBC.
Cha
M K
MK
Department of Biochemistry, Pai-Chai University, Taejon, Republic of Korea.
Kim
I H
IH
D000595:Amino Acid Sequence; D001798:Blood Proteins / Q000737:chemistry; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D009249:NADP / Q000378:metabolism; D009363:Neoplasm Proteins; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000737:chemistry; D010544:Peroxidases / Q000097:blood*; D061105:Peroxiredoxin III; D054464:Peroxiredoxins; D011506:Proteins / Q000737:chemistry*; D013880:Thioredoxin-Disulfide Reductase / Q000097:blood*; D013879:Thioredoxins / Q000097:blood*
D001798:Blood Proteins; D009363:Neoplasm Proteins; D010446:Peptide Fragments; D011506:Proteins; D013879:Thioredoxins; D009249:NADP; D010544:Peroxidases; C516115:PRDX3 protein, human; D061105:Peroxiredoxin III; D054464:Peroxiredoxins; D013880:Thioredoxin-Disulfide Reductase