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۱Interaction of Secreted Aspartic Proteinase Candida albicans with ZnCl2: Complex Formation and Catalytic Activity
اطلاعات انتشار: World Applied Sciences Journal، بيست و هفتم،شماره۹، ۲۰۱۳، سال
تعداد صفحات: ۵
The aim of work is to estimate ion Zn(II) influence on catalytic activity of secreted aspartic proteinase Candida albicans (SAP2). System ZnCl2 – SAP2 showed complex formation. Composition of [ZnmSAP2n ] complex was 1:1, the stability constant was 4.73±0.20. Affinity constants in system SAP – human serum albumin (HSA) – ZnCl2 were determined at Skatchard coordinates. The SAP2 was found to have a one section for linking with the substrate and one section for linking with modulator. The affinity constants in SAP2 – HSA system decreased in presence of ZnCl2. Complex forming of SAP2 – ZnCl2 system resulted in reduction of enzyme–substrate bonding. Proteolytic activity of SAP2 towards HSA at presence ZnCl2 as modulator was estimated. The inhibition effect in range 1×10 4 – 4×10 6 and 6×10 7 – 1×10 8 M was observed. The SAP2 activation effect catalyzed by ZnCl2 at 5×10 – 5×10 M concentrations were fixed for the first time.
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