Grabert E, Wingender J, Winkler U K
Lehrstuhl für Biologie der Mikroorganismen, Ruhr-Universität Bochum, F.R.G.
FEMS Microbiol Lett. 1990 Mar 1;56(1-2):83-7. doi: 10.1111/j.1574-6968.1990.tb04127.x.
SDS-polyacrylamide gel electrophoresis of outer membrane (OM) proteins of different mucoid strains of P. aeruginosa revealed a protein of about 54 kDa that was absent in nonmucoid strains. This 54 kDa protein was expressed under iron-restricted and iron sufficient growth conditions. Electrophoretic mobility of the 54 kDa protein was modified by the solubilization temperature as well as by the addition of lipopolysaccharide and alginate prior to electrophoresis. Treatment of OMs with octylglucoside/KCl or SDS completely extracted the 54 kDa protein at low temperatures. The possible role of this protein in biosynthesis and/or excretion of bacterial alginate is discussed.
对不同黏液型铜绿假单胞菌菌株的外膜(OM)蛋白进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示,存在一种约54 kDa的蛋白,该蛋白在非黏液型菌株中不存在。这种54 kDa的蛋白在铁限制和铁充足的生长条件下均有表达。54 kDa蛋白的电泳迁移率会因溶解温度以及电泳前添加脂多糖和藻酸盐而发生改变。用辛基葡糖苷/氯化钾或十二烷基硫酸钠处理外膜,在低温下能完全提取出54 kDa的蛋白。本文讨论了该蛋白在细菌藻酸盐生物合成和/或分泌中的可能作用。