Ys. Lim et al., PURIFICATION AND CHARACTERIZATION OF THIOL-SPECIFIC ANTIOXIDANT PROTEIN FROM HUMAN RED-BLOOD-CELL - A NEW-TYPE OF ANTIOXIDANT PROTEIN, Biochemical and biophysical research communications, 199(1), 1994, pp. 199-206
A thiol-specific antioxidant protein (Protector Protein, PRP) was puri
fied from human red blood cells (RBC). The PRP exists as a predominant
protein in human RBC, which showed distinct thiol-specific antioxidan
t activities in the presence of dithiothreitol (DTT) as a reducing equ
ivalent, The human RBC PRP (HRPRP) completely inhibited visible absorp
tion spectral changes of oxyhemoglobin, DNA cleavage, and the peroxida
tion of RBC membrane by a nonenzymatic Fe3+/O-2/thiol mixed-function o
xidation system capable of generating hydroxyl radical. These observat
ions suggest that HRPRP could act as a new type of antioxidant protein
to maintain the RBC integrity by scavenging reactive oxygen species.
(C) 1994 Academic Press, Inc.