A review is presented of the scientific literature on the effects of sugars (mono- and disaccharides), when used as tobacco additives, on the formation of acetaldehyde in mainstream (MS) smoke and the potential bioavailablity of MS smoke acetaldehyde derived from sugars to the smoker. The experimental data supports the following conclusions. Sugars, e.g., D-glucose, D-fructose, and sucrose, do not produce greater yields of acetaldehyde in MS smoke than are produced from tobacco itself on a weight-for-weight basis. A variety of studies suggests that natural tobacco polysaccharides, including cellulose, are the primary precursors of acetaldehyde in MS smoke. In a number of different studies using commercial cigarette brands, MS smoke yields of acetaldehyde correlate (r > 0.9) with both MS smoke "tar" and carbon monoxide. MS smoke acetaldehyde yields are affected more by cigarette design characteristics that influence total smoke production, such as filter ventilation, filtration, and paper porosity, than by reducing sugars. MS smoke acetaldehyde deposits primarily in the upper respiratory tract, including the mouth, of the smoker. Acetaldehyde is rapidly metabolized by aldehyde dehydrogenase in the blood and elsewhere in the body, including at the blood-brain barrier. Tobacco sugar-derived MS smoke acetaldehyde from commercial cigarettes is unlikely to result in direct central nervous system effects on the smoker.
A sensitive and reliable assay method was developed to characterize crude cell homogenates and subcellular fractions with regard to their superoxide dismutase (SOD) activities. The determination of SOD activities was based on the well-known spectrophotometric assay introduced by McCord & Fridovich [(1969) J. Biol. Chem. 244, 6049-6055], with partially succinylated (3-carboxypropionylated) rather than native ferricytochrome c as indicating scavenger. Partial succinylation of cytochrome c resulted in minimization of interference associated with the interaction of cytochrome c with mitochondrial cytochrome c oxidase or cytochrome c reductases. The further increase in specificity, with regard to exclusion of cytochrome c oxidase interference, gained as a consequence of the high pH of 10 enabled the analysis of samples as rich in cytochrome c oxidase activity as the mitochondrial fraction in the presence or absence of membrane-disrupting detergents. Linear relationships for the dependence of the SOD activities with protein concentration were obtained with rat liver homogenate, mitochondrial and microsomal fractions, indicating negligible interference. Furthermore, by choosing a high pH for the assay medium, a 4-fold increase in sensitivity compared with the classical SOD assay, carried out at pH 7.8, was gained as well as a more precise resolution of Cu/Zn-SOD and Mn-SOD by 2 mM-KCN in samples with a high ratio of Mn-SOD to Cu/Zn-SOD, such as mitochondria. The complete trapping of the O2.- radicals, which was more feasible at pH 10 than at pH 7.8, enabled the application of a simple equation derived for the calculation of appropriately defined units of SOD activity from a single experiment.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.