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Enzymes Produced by a Pseudomonas Species Which Inactivate Inhibitors of Certain Viral Hemagglutinins. I. Identification and Purification of a Proteinase and Phospholipase C

机译:由假单胞菌属物种产生的酶,可以使某些病毒血凝素的抑制剂失活。 I.蛋白酶和磷脂酶C的鉴定和纯化

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Filtrates from cultures of a psychrophilic Pseudomonas species, which inactivate serum inhibitors of certain viral hemagglutinins, were shown to contain both lecithinase (phospholipase C) and a proteolytic enzyme with elastase activity. The bacterium was cultivated under conditions favoring production of the respective enzymes, and the enzymes were purified by ammonium sulfate precipitation followed by column chromatography or by gel filtration. The elastase was obtained in crystalline form and was recrystallized. It has properties similar to those of a number of other bacterial elastases but is more heat-labile than most. Although a high degree of purification was achieved for the lecithinase, as evidenced by an increase in specific activity, it was not obtained in crystalline form. Partially purified preparations of the lecithinase had extremely high activity compared to that of commercial preparations of phospholipase C from Clostridium welchii.
机译:嗜冷假单胞菌菌种的滤液使某些病毒血凝素的血清抑制剂失活,显示含有卵磷脂酶(磷脂酶C)和具有弹性蛋白酶活性的蛋白水解酶。在有利于产生各种酶的条件下培养细菌,并通过硫酸铵沉淀,然后通过柱色谱或通过凝胶过滤来纯化酶。获得了结晶形式的弹性蛋白酶,并将其重结晶。它具有与许多其他细菌弹性蛋白酶相似的特性,但比大多数细菌更不稳定。尽管卵磷脂酶可实现高度纯化,如比活性增加所证明,但并非以结晶形式获得。与来自魏氏梭状芽胞杆菌的磷脂酶C的商业制剂相比,部分纯化的卵磷脂酶制剂具有极高的活性。

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