Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo.
Thiol-specific antioxidant protein (Protector Protein; PRP) from Saccharomyces cerevisiae was found to remove hydrogen peroxide and hydroxyl radical in the presence of dithiothreitol (DTT). Without DTT as a reducing equivalent, the antioxidant protein did not show the activities for destroying hydrogen peroxide and hydroxyl radical. N-ethylmaleimide (NEM) was observed to prevent the PRP from both removing hydrogen peroxide and protecting the cleavage of DNA. These observations suggest that the sulfhydryl of cysteine in PRP could function as a strong nucleophile to attack and destroy H2O2 and .OH.
Department of Biochemistry, Pai-Chai University, Taejon, Republic of Korea.
Y S
YS
Lim
M K
MK
Cha
H K
HK
Kim
T B
TB
Uhm
J W
JW
Park
K
K
Kim
I H
IH
Kim
D000975:Antioxidants / Q000378:metabolism*; D016166:Free Radical Scavengers; D005656:Fungal Proteins / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D006878:Hydroxides / Q000378:metabolism*; D017665:Hydroxyl Radical; D009363:Neoplasm Proteins; D010544:Peroxidases; D054464:Peroxiredoxins; D017382:Reactive Oxygen Species / Q000378:metabolism
D000975:Antioxidants; D016166:Free Radical Scavengers; D005656:Fungal Proteins; D006878:Hydroxides; D009363:Neoplasm Proteins; D017382:Reactive Oxygen Species; D017665:Hydroxyl Radical; D006861:Hydrogen Peroxide; D010544:Peroxidases; D054464:Peroxiredoxins