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Secretion of phospholipase C by Pseudomonas aeruginosa.

机译:铜绿假单胞菌分泌磷脂酶C。

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The conditions necessary for the secretion of phospholipase C (phosphatidylcholine cholinephosphohydrolase) by Pseudomonas aeruginosa were studied. Enzyme secretion by washed cell suspensions required a carbon source and ammonium, potassium, and calcium ions. The calcium requirement could be substituted by magnesium and strontium but not by copper, manganese, cobalt, or zinc. During growth in liquid medium, cells secreted phospholipase C during late logarithmic and early stationary phases. Secretion was repressed by the addition of inorganic phosphate but not by organic phosphates, glucose, or sodium succinate. Studies with tetracycline indicated that de novo protein synthesis was necessary for the secretion of phospholipase C and that the exoenzyme was not released from a preformed periplasmic pool. Similarly, extraction of actively secreting cells with 0.2 M MgCl2 at pH 8.4 solubilized large quantities of the periplasmic enzyme alkaline phosphatase but insignificant amounts of phospholipase C. Bacteria continued to secrete enzyme for nearly 45 min after the addition of inorganic phosphate or rifampin.
机译:研究了铜绿假单胞菌分泌磷脂酶C(磷脂酰胆碱胆碱磷酸水解酶)的必要条件。洗涤过的细胞悬液分泌的酶需要碳源以及铵,钾和钙离子。钙需要量可以用镁和锶代替,但不能用铜,锰,钴或锌代替。在液体培养基中生长期间,细胞在对数后期和静止初期分泌磷脂酶C。通过添加无机磷酸盐抑制分泌,但不通过有机磷酸盐,葡萄糖或琥珀酸钠抑制分泌。用四环素进行的研究表明,从头合成蛋白质是分泌磷脂酶C所必需的,并且外切酶没有从预先形成的周质池中释放。同样,在pH 8.4下用0.2 M MgCl2提取活跃分泌的细胞可溶解大量的周质酶碱性磷酸酶,但微不足道的磷脂酶C。细菌在加入无机磷酸盐或利福平后持续分泌酶近45分钟。

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