Naja venom Lamino acid oxidase Purification physical chemical and enzymatic properties.doc
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Naja venom Lamino acid oxidase Purification physical chemical and enzymatic properties
PAGE \* MERGEFORMAT 13
Naja venom Lamino acid oxidase Purification physical chemical and enzymatic properties
Author: Lin Li Shan, Zhang Zhiqiang, Chen Zhou, XU Yun-lu
[Abstract] Objective isolated from Naja atra venom L amino acid oxidase (LAO), measured by physical and chemical and enzymatic properties. Methods Sephadex G 100 gel chromatography and POROS CM20 ion-exchange chromatography separation and purification LAO; Wellner and Lichtenberg Determination of LAO activity; SDS PAGE Determination of relative molecular mass. Results Naja atra venom by Sephadex G 100 gel chromatography and two POROS 20 ion-exchange chromatography and obtained pure LAO (tentative name NA LAO). NA LAO in the non-reducing and reducing conditions are the molecular weight of about 58 kD; its response to the optimal pH is 8.0, the optimum temperature is 60 ℃ , right L phenylalanine Michaelis constant (Km) 3.08 mmoL / L. Conclusion gel filtration chromatography and ion-exchange chromatography from the venom of Naja purified LAO.
[Keywords:] cobra venoms; amino acid reductase
Venom component complex, mainly enzymes and toxins, L amino acid oxidase (EC.1.4.3.2) are widely distributed in the venom, in the Viperidae, rattlesnakes Branch, cobra, viper branches in the Section, and are distributed [1 4 ]. L amino acid oxidase (L amino acid oxidase, LAO) is an important activity of venom components, could catalyze the oxidation of L amino acid deamination reaction of the corresponding α acid, ammonia and hydrogen peroxide [ 5], with a variety of biological activities, such as vascular endothelial cells induced apoptosis, inhibit or induce platelet aggregation, cell toxicity and antibacterial activity of [6 10]. Several isolated from snake venom LAO, I use gel chromatography and ion-exchange chromatography separated from Naja atra venom LAO, and on some of the physico-chemical and enzymatic properties of a preliminary study.
1 Materials and met
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