http://nopr.niscair.res.in/handle/123456789/3231 Search the Channel search http://nopr.niscair.res.in/simple-search http://nopr.niscair.res.in/handle/123456789/3260 Title: Enzymatic characteristics of ligninperoxidases from Penicillium citrinum, Fusarium oxysporum and Aspergillus terreus using n-propanol as substrate <br/> <br/>Authors: Yadav, Meera; Yadav, K D S <br/> <br/>Abstract: The activities of ligninperoxidases from Penicillium citrinum MTCC 3565, Fusarium oxysporum MTCC 3379 and Aspergillus terreus MTCC 3374 have been assayed and the enzymatic characteristics like Km, pH and temperature optima using n-propanol as the substrate have been reported. The results suggest that n-propanol can substitute veratryl alcohol as substrate for assaying ligninperoxidase activities from different fungal strains, without affecting the enzymatic characteristics. The above strains were selected, as they were known to secrete ligninperoxidase in the liquid culture medium. <br/> <br/>Page(s): 48-51 http://nopr.niscair.res.in/handle/123456789/3259 Title: Development of pharmacophoric model of condensed pyridine and pyrimidine analogs as hydroxymethyl glutaryl coenzyme A reductase inhibitors <br/> <br/>Authors: Saxena, M; Soni, Love K; Gupta, Arun K; Wakode, S R; Saxena, A K; Kaskhedikar, S G <br/> <br/>Abstract: Quantitative structure-activity relationship (QSAR) has been established on a series of thirty-eight compounds of four different sets of condensed pyridine and pyrimidine analogs, for their hydroxymethyl glutaryl coenzyme (HMG-CoA) reductase inhibitor activity, in order to understand the essential structural requirement for binding with receptor, in terms of common biophoric and secondary sites employing APEX-3D software. Among several 3D pharmacophoric models with different sizes and arrangements, one model was selected based on r² = 0.8, chance<0.001, match equivalent to 0.38 and all the 38 compounds were considered. The results suggest that hydrophobicity, hydrogen acceptor and optimum steric refractivity play a dominant role in the inhibition of HMG-CoA reductase. The information obtained from the present study can be used to design and predict more potent molecules as HMG-CoA reductase inhibitors, prior to their synthesis. <br/> <br/>Page(s): 32-36 http://nopr.niscair.res.in/handle/123456789/3257 Title: Effect of vitamin E on monosodium glutamate induced hepatotoxicity and oxidative stress in rats <br/> <br/>Authors: Onyema, Oscar Okwudiri; Farombi, Ebenezer Olatunde; Emerole, Godwin O; Ukoha, Agwu Igwe; Onyeze, Godffrey Okeke <br/> <br/>Abstract: Monosodium glutamate (MSG), administered to rats (by gavage) at a dose of 0.6 mg/g body weight for 10 days, significantly {P<0.05) induced lipid peroxidation (LPO), decreased reduced glutathione (GSH) level and increased the activities of glutathione-s-transferase (GST), catalase and superoxide dismutase (SOD) in the liver of the animals; these were observed 24 hr after 10 days of administration. The activities of alanine aminotransferase (ALT), aspartate aminotransferase (AST) and ϒ glutamyl transferase (GGT) were also significantly increased in the serum, on MSG administration. Vitamin E (0.2 mg/g body wt) co-administered with MSG, significantly reduced the LPO, increased the GSH level and decreased the hepatic activities of GST, catalase and SOD. The activities of ALT, AST and GGT in the serum were also significantly reduced. The results showed that MSG at a dose of 0.6 mg/g body wt induced the oxidative stress and hepatotoxicity in rats and vitamin E ameliorated MSG-induced oxidative stress and hepatotoxicity. <br/> <br/>Page(s): 20-24 http://nopr.niscair.res.in/handle/123456789/3255 Title: Kinetics and mechanism of reduction of ferricytochrome c by glutathione and L-cysteine: A comparative study <br/> <br/>Authors: Subudhi, U; Chainy, G B N; Mohanty, P <br/> <br/>Abstract: The kinetics and mechanism of the reduction of ferricytochrome c [Cyt c(III)] by substrates namely glutathione (GSH) and L-cysteine (L-cys) have been investigated spectrophotometrically employing [substrate]T >> [Cyt c(III)]T. The reaction exhibits first order dependence in [substrate]T and [Cyt c(III)]T. The pseudo-first order rate constant increases with an increase in pH, indicating that the conjugate base form of the HCyt c(III) is a better oxidant than the parent HCyt c(III). The electron transfer rate constants between the oxidants and GSH for both the k₁ and k₂ paths are found to be greater than that with L-cysteine. Hence, GSH is a better reductant of Cyt c(III) as compared to L-cysteine. A suitable mechanism has been proposed on the basis of experimental findings. The deprotonation constant for HCyt c(III) and the second order rate constants of k₁ and k₂ paths for the present reaction at 25ºC have been determined. <br/> <br/>Page(s): 37-40