Goullet P, Picard B
J Gen Microbiol. 1986 Jul;132(7):1843-51. doi: 10.1099/00221287-132-7-1843.
To determine whether enzyme electrophoretic polymorphism in Escherichia coli populations was influenced by environmental background, the mobilities of four electrophoretically variable esterases (A, B, C and I) were examined. The distinction between isolates was established by significant differences in the electrophoretic distribution and the genetic diversity coefficient of individual esterases. Principal components analysis on each population and on all strains revealed three groups of allozymes. The first, characterized by slow electrophoretic mobilities of esterase B, was frequently observed in strains obtained from human extra-intestinal infections and rarely in commensal organisms. The second, characterized by fast mobilities of esterases A and B, was frequently found in animal isolates. The third, characterized by prominence of the most common mobilities of esterases B and A, was recovered in all populations. These results were confirmed by discriminant analysis. Among the 610 strains investigated, 316 electrophoretic types (distinctive combinations of allozymes of the four varieties of esterases) were distinguished, illustrating high esterase polymorphism.
为了确定大肠杆菌群体中的酶电泳多态性是否受环境背景影响，研究了四种电泳可变酯酶（A、B、C和I）的迁移率。通过个体酯酶电泳分布和遗传多样性系数的显著差异来区分分离株。对每个群体和所有菌株进行主成分分析，揭示了三组同工酶。第一组以酯酶B的电泳迁移率较慢为特征，常见于从人类肠道外感染中分离出的菌株，而在共生生物中很少见。第二组以酯酶A和B的迁移率较快为特征，常见于动物分离株。第三组以酯酶B和A最常见迁移率的突出为特征，在所有群体中都有发现。判别分析证实了这些结果。在所研究的610株菌株中，区分出316种电泳类型（四种酯酶同工酶的独特组合），表明酯酶具有高度多态性。
