Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein

Biochem Biophys Res Commun. 1994 Feb 28;199(1):199-206. doi: 10.1006/bbrc.1994.1214.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antioxidants*
  • Blood Proteins / chemistry*
  • Erythrocytes / chemistry*
  • Fungal Proteins / blood*
  • Hemoglobins / chemistry
  • Humans
  • Lipid Peroxides / chemistry
  • Neoplasm Proteins*
  • Oxidation-Reduction
  • Peroxidases*
  • Peroxiredoxin III
  • Peroxiredoxins
  • Sulfhydryl Compounds / chemistry


  • Antioxidants
  • Blood Proteins
  • Fungal Proteins
  • Hemoglobins
  • Lipid Peroxides
  • Neoplasm Proteins
  • Sulfhydryl Compounds
  • Peroxidases
  • PRDX3 protein, human
  • Peroxiredoxin III
  • Peroxiredoxins