salicylates and quinone

Whereas the parent uranyl salophen is catalytically inactive, its phenyl derivative effectively catalyses with turnover the reaction of benzoquinone with 1,3-cyclohexadiene, while showing no appreciable affinity towards reactants and product.

Topics: Benzoquinones; Catalysis; Ketones; Kinetics; Molecular Structure; Organometallic Compounds; Phase Transition; Salicylates

In vitro and in vivo studies were made with an alcohol extract of the seeds of Mucuna pruriens (Fabaceae) to investigate its antioxidant property. In vitro studies were carried out in rat liver homogenate to investigate the chemical interaction of various phytochemicals with different species of free radicals. The effect was also checked on iron-induced lipid peroxidation, oxidation of GSH content, and its interaction with hydroxyl and superoxide radicals. There was no change on the rate of aerial oxidation of GSH content but it significantly inhibited FeSO(4) induced lipid peroxidation. It also inhibited the specific chemical reactions induced by superoxides and hydroxyl radicals. The removal of these species was through direct chemical interaction. An in vivo study on albino rats for 30 days showed no toxic effect up to a dose of 600 mg/kg body weight, on oral administration. There was no change in the level of TBA-reactive substances, reduced glutathione content and SOD activity in the liver. The activity of serum GOT, GPT and alkaline phosphatase was also unchanged. Thus it could be concluded that the alcohol extract of the seeds of M. pruriens has an antilipid peroxidation property, which is mediated through the removal of superoxides and hydroxyl radicals.

Topics: Alanine Transaminase; Animals; Aspartate Aminotransferases; Benzoquinones; Chlorides; Copper Sulfate; Fabaceae; Free Radical Scavengers; Glutathione; Hydroxylation; Lipid Peroxidation; Liver; Manganese Compounds; Oxidative Stress; Plant Extracts; Rats; Salicylates; Seeds; Superoxides; Vitamin E

Salicylate was found to uniquely induce a 27-kDa protein in Mycobacterium tuberculosis complex organisms but not in Mycobacterium smegmatis or Escherichia coli. The structural analogue antitubercular para-amino-salicylate also induced the 27-kDa protein but to a somewhat lower level than salicylate. Other structural analogues such as benzoic acid and acetyl salicylic acid (aspirin) did not induce the 27-kDa protein. Western blot analysis indicated that the 27-kDa protein was localized mainly in the cytoplasm. The 27-kDa protein was not expressed at different growth phases in the absence of salicylate. The 27-kDa protein was identified as a putative benzoquinone methyltransferase (Rv0560c), which has several homologues in the M. tuberculosis genome. The cloned 27-kDa gene was found to express constitutively in E. coli, M. smegmatis and BCG with or without salicylate.

Topics: Aminosalicylic Acid; Bacterial Proteins; Benzoquinones; Culture Media; Enzyme Induction; Methyltransferases; Mycobacterium tuberculosis; Salicylates