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Pb~(2+) Inhibits Competitively Flocculation of Saccharomyces cerevisiae

机译:Pb〜(2+)竞争抑制酿酒酵母的絮凝

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Pb~(2+) inhibited calcium-induced flocculation in Flo1 (S646-1B) and NewFlo phenotype strains (NCYC 1190, NCYC 1195 and NCYC 1364) of Saccharomyces cerevisiae. Flocculation was restored after washing with water or EDTA, which suggests a reversible binding of Pb~(2+) to yeast cell walls. Pb~(2+) probably inhibited flocculation by competing with Ca~(2+), since Pb~(2+) inhibition was alleviated by excess of Ca~(2+). Using a fluorescent avidin-fluorescein isothiocyanate (Avidin-FITC) probe, active cell surface flocculation lectins, in the presence of Ca~(2+) ions, were visualized. Conversely, Avidin-FITC was not fixed to yeast walls of flocculent cells, in the presence of Pb~(2+) ions or in the simultaneous presence of 0.05 mM Ca~(2+) and 0.4 mM Pb~(2+). These results suggest that Pb~(2+) ions were not able to induce the correct conformation of the lectin-like component and reinforces the hypothesis that Pb~(2+) ions compete for the same "calcium site" of flocculation zymolectins.
机译:Pb〜(2+)抑制了酿酒酵母Flo1(S646-1B)和NewFlo表型菌株(NCYC 1190,NCYC 1195和NCYC 1364)中钙诱导的絮凝。用水或EDTA洗涤后絮凝得以恢复,这表明Pb〜(2+)与酵母细胞壁可逆结合。由于过量的Ca〜(2+)减轻了Pb〜(2+)的抑制作用,因此Pb〜(2+)可能通过与Ca〜(2+)竞争而抑制了絮凝。使用荧光亲和素-异硫氰酸荧光素(Avidin-FITC)探针,在存在Ca〜(2+)离子的情况下,可以看到活性细胞表面絮凝凝集素。相反,在存在Pb〜(2+)离子或同时存在0.05 mM Ca〜(2+)和0.4 mM Pb〜(2+)的情况下,抗生物素蛋白-FITC不能固定在絮状细胞的酵母壁上。这些结果表明,Pb〜(2+)离子不能诱导凝集素样成分的正确构象,并加强了Pb〜(2+)离子竞争絮凝酶连接素的相同“钙位点”的假设。

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