Commenced in January 2007
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Edition: International
Paper Count: 3

specificity Related Publications

3 Role of Fish Hepatic Aldehyde Oxidase in Oxidative in vitro Metabolism of Phenanthridine Heterocyclic Aromatic Compound

Authors: Khaled S. Al Salhen

Abstract:

Aldehyde oxidase is molybdo-flavoenzyme involved in the oxidation of hundreds of endogenous and exogenous and N-heterocyclic compounds and environmental pollutants. Uncharged N-heterocyclic aromatic compounds such phenanthridine are commonly distributed pollutants in soil, air, sediments, surface water and groundwater, and in animal and plant tissues. Phenanthridine as uncharged N-heterocyclic aromatic compound was incubated with partially purified aldehyde oxidase from rainbow trout fish liver. Reversed-phase HLPC method was used to separate the oxidation products from phenanthridine and the metabolite was identified. The 6(5H)-phenanthridinone was identified the major metabolite by partially purified aldehyde oxidase from fish liver. Kinetic constant for the oxidation reactions were determined spectrophotometrically and showed that this substrate has a good affinity (Km = 78 ± 7.6µM) for hepatic aldehyde oxidase, will be a significant pathway. This study confirms that partially purified aldehyde oxidase from fish liver is indeed the enzyme responsible for the in vitro production 6(5H)-phenanthridinone metabolite as it is a major metabolite by mammalian aldehyde oxidase, coupled with a relatively high oxidation rate (0.77± 0.03 nmol/min/mg protein). In addition, the kinetic parameters of hepatic fish aldehyde oxidase towards the phenanthridine substrate indicate that in vitro biotransformation by hepatic fish aldehyde oxidase will be a significant pathway. This study confirms that partially purified aldehyde oxidase from fish liver is indeed the enzyme responsible for the in vitro production 6(5H)-phenanthridinone metabolite as it is a major metabolite by mammalian aldehyde oxidase.

Keywords: Fish, aldehyde oxidase, phenanthridine, specificity

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2 Lipase Catalyzed Synthesis of Aromatic Esters of Sugar Alcohols

Authors: R. Croitoru, F. Peter, C. G. Boeriu, A. E. Frissen, C. M. Davidescu, L. A. M. van den Broek

Abstract:

Commercially available lipases (Candida antarctica lipase B, Novozyme 435, Thermomyces lanuginosus lipase, and Lipozyme TL IM), as well as sol-gel immobilized lipases, have been screened for their ability to acylate regioselectively xylitol, sorbitol, and mannitol with a phenolic ester in a binary mixture of t-butanol and dimethylsulfoxide. HPLC and MALDI-TOF MS analysis revealed the exclusive formation of monoesters for all studied sugar alcohols. The lipases immobilized by the sol-gel entrapment method proved to be efficient catalysts, leading to high conversions (up to 60%) in the investigated acylation reactions. From a sequence of silane precursors with different nonhydrolyzable groups in their structure, the presence of octyl and i-butyl group was most beneficial for the catalytic activity of sol-gel entrapped lipases in the studied process.

Keywords: transesterification, specificity, lipase, phenolic ester, sugar alcohol

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1 Autobiographical Memory and Flexible Remembering: Gender Differences

Authors: A. Aizpurua, W. Koutstaal

Abstract:

In this study, we examined gender differences in: (1) a flexible remembering task, that asked for episodic memory decisions at an item-specific versus category-based level, and (2) the retrieval specificity of autobiographical memory during free recall. Differences favouring women were found on both measures. Furthermore, a significant association was observed, across gender groups, between level of specificity in the autobiographical memory interview and sensitivity to gist on the flexible remembering task. These results suggest that similar cognitive processes may partially contribute to both the ability for specific autobiographical recall and the capacity for inhibition of gist-information on the flexible remembering task.

Keywords: Gender, specificity, autobiographical memory, flexible remembering

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