Schmidt N J, Gee P S, Dennis J, Lennette E H
Appl Microbiol. 1969 Sep;18(3):500-8. doi: 10.1128/am.18.3.500-508.1969.
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.
从一种嗜冷假单胞菌属菌株的培养物滤液中发现，该滤液能使某些病毒血凝素的血清抑制剂失活，其中含有卵磷脂酶（磷脂酶C）和一种具有弹性蛋白酶活性的蛋白水解酶。在有利于产生相应酶的条件下培养该细菌，然后通过硫酸铵沉淀，接着进行柱色谱或凝胶过滤来纯化这些酶。弹性蛋白酶以结晶形式获得并进行了重结晶。它具有与许多其他细菌弹性蛋白酶相似的特性，但比大多数弹性蛋白酶更不耐热。尽管通过比活性的增加证明卵磷脂酶已达到高度纯化，但未获得结晶形式。与产气荚膜梭菌的商业磷脂酶C制剂相比，部分纯化的卵磷脂酶制剂具有极高的活性。
