Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein.
A thiol-specific antioxidant protein (Protector Protein, PRP) was purified from human red blood cells (RBC). The PRP exists as a predominant protein in human RBC, which showed distinct thiol-specific antioxidant activities in the presence of dithiothreitol (DTT) as a reducing equivalent. The human RBC PRP (HRPRP) completely inhibited visible absorption spectral changes of oxyhemoglobin, DNA cleavage, and the peroxidation of RBC membrane by a nonenzymatic Fe3+/O2/thiol mixed-function oxidation system capable of generating hydroxyl radical. These observations suggest that HRPRP could act as a new type of antioxidant protein to maintain the RBC integrity by scavenging reactive oxygen species.
Lim
Y S
YS
Department of Biochemistry, Pai-Chai University, Taejon, Republic of Korea.
Cha
M K
MK
Yun
C H
CH
Kim
H K
HK
Kim
K
K
Kim
I H
IH
D000975:Antioxidants; D001798:Blood Proteins / Q000737:chemistry*; D004912:Erythrocytes / Q000737:chemistry*; D005656:Fungal Proteins / Q000097:blood*; D006454:Hemoglobins / Q000737:chemistry; D006801:Humans; D008054:Lipid Peroxides / Q000737:chemistry; D009363:Neoplasm Proteins; D010084:Oxidation-Reduction; D010544:Peroxidases; D061105:Peroxiredoxin III; D054464:Peroxiredoxins; D013438:Sulfhydryl Compounds / Q000737:chemistry
D000975:Antioxidants; D001798:Blood Proteins; D005656:Fungal Proteins; D006454:Hemoglobins; D008054:Lipid Peroxides; D009363:Neoplasm Proteins; D013438:Sulfhydryl Compounds; D010544:Peroxidases; C516115:PRDX3 protein, human; D061105:Peroxiredoxin III; D054464:Peroxiredoxins