Cynthia N. Oliver

TL;DR: This chapter discusses methods to determine carbonyl content in oxidatively modified proteins and quantitated protein-bound pyruvoyl groups through formation of a Schiff base with p-aminobenzoic acid followed by reduction with cyanoborohydride.

TL;DR: It is concluded that protein oxidation products accumulate in the brain and that oxidation-vulnerable enzyme activities decrease with aging in the same regional pattern (frontal more affected than occipital) and that AD may represent a specific brain vulnerability to age-related oxidation.

TL;DR: It is reported that free radical flux is increased during the reperfusion phase of the ischemia-lesioned gerbil brain, and the free radical spin trap N-tert-butyl-alpha-phenylnitrone-dependent nitroxide radical obtained in the lipid fraction.

TL;DR: It is suggested that mixed-function oxidation system-catalyzed inactivation of enzymes is a regulatory step in enzyme turn-over and the implication of oxidative inactivation reactions in ageing is suggested by the fact that many of the enzymes inactivated by mixed- function oxidation systems are known to accumulate as inactive forms during ageing.

TL;DR: The possible relationship between protein oxidation and proteolysis during aging and oxidative stress in vivo is investigated and the increase in protein oxidation is correlated with a loss of specific activity of GS and G-6-PDH without a concomitant loss of immunological cross-reactivity.