Modification of proteins and polynucleotides by peroxynitrite.
Varied intensities of nitrotyrosine immunoreactivity were detected by Western blots after the reaction of proteins or enzymes with peroxynitrite (PN), a strong oxidant derived from nitric oxide. Intense immunoreactivity of cAMP-dependent protein kinase, calmodulin and most histones may depend on greater access to tyrosine residues in the reaction, whereas the absence of immunoreactivity of caspase-3, ubiquitin and S-100 proteins may reflect lack of accessibility. In addition, the changes in UV/visible absorbency were observed after PN-treatment of polynucleotides, polypeptides or proteins. Brief PN-treatment of invertase increased its enzymatic activity. Furthermore, PN-treatment of rabbit IgG decreased its recognition by anti-IgG. The results suggest that PN may chemically modify polypeptides, proteins and polynucleotides and may subsequently alter their biological activity.
Kuo
W N
WN
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114, USA.
Kanadia
R N
RN
Shanbhag
V P
VP
Morgan
R
R
D000818:Animals; D009566:Nitrates / Q000737:chemistry* / Q000378:metabolism; D009569:Nitric Oxide / Q000737:chemistry / Q000378:metabolism; D016877:Oxidants / Q000737:chemistry* / Q000378:metabolism; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D011817:Rabbits; D014443:Tyrosine / Q000031:analogs & derivatives / Q000032:analysis / Q000276:immunology
D009566:Nitrates; D016877:Oxidants; D011506:Proteins; C039642:peroxynitric acid; D009569:Nitric Oxide; C002744:3-nitrotyrosine; D014443:Tyrosine