Importance of thiols in the reductive binding of 2-nitroimidazoles to macromolecules.
Reductive activation of 2-nitroimidazoles in the presence of bovine serum albumin (BSA) led to binding of the nitroheterocycles to the protein. The binding was most efficient to BSA in which protein disulfides had been reduced to thiol groups. Protein thiols were at least twenty times more efficient than other protein, RNA or DNA nucleophiles in binding the reductively-activated nitroheterocycles. This result is of practical importance in the development of immunoassays for 2-nitroimidazoles as hypoxia markers in normal and tumor tissue.
Raleigh
J A
JA
Radiation Oncology Department, University of North Carolina Hospitals, Chapel Hill 27599-7512.
Koch
C J
CJ
D006037:Glyoxal / Q000378:metabolism; D006878:Hydroxides; D017665:Hydroxyl Radical; D009593:Nitroimidazoles / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000494:pharmacology; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000378:metabolism*
D006878:Hydroxides; D009593:Nitroimidazoles; D013438:Sulfhydryl Compounds; D012710:Serum Albumin, Bovine; D017665:Hydroxyl Radical; D006037:Glyoxal; D010100:Oxygen