formation of strongostrong-tyrosine and dityrosine in proteins during.pdfVIP

THEJOURNALOF BIOLOGICALCHEMISTRY Vol. 268, No. 17, Issue of June 15,pp. 12341-12347,1993 Printed in U.S.A. 0 1993 by The American Society for Biochemistry and Molecular Biology, Inc. Formation of o-Tyrosine and Dityrosine in Proteinsduring Radiolytic and Metal-catalyzed Oxidation* (Received for publication, December 22, 1992, and in revised form, February 26,1993) Thomas G. Huggins$, Mary C.Wells-KnechtS, Nicholas A. Detoriej, John W. BaynesSll, and Suzanne R. ThorpeSJI From the $Departmentof Chemistry and Biochemistry and the llSchool of Medicine, University of South Carolina, Columbia, South Carolina29208 and the §Departmentof Medical Physics, Richland Memorial Hospital, Columbia, South Carolina 29208 To evaluate their usefulness as chemical indicators sion injury (2). However, only trace levels of carbonyl com- of cumulative oxidative damage to proteins, we studied pounds are detectable in tissue proteins,undoubtedly because the kinetics and extent of formation of ortho-tyrosine of the reactivity of aldehydes and ketones with nucleophiles (0-Tyr), dityrosine (DT), and dityrosine-like fluores- under physiological conditions. Increases in levels of these cence (Ex=3 17 nm,E,,, =407 nm)in the model proteins compounds with age and pathological conditions are also RNase and lysozyme exposed to radiolytic and metal- limited, generally less than %fold, consistent with their re- catalyzed (H20z/Cu2+)oxidation (MCO). Although