Sawa Y, Shibata K, Watanabe T
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Japan.
FEMS Microbiol Lett. 1995 Apr 15;128(1):9-14. doi: 10.1111/j.1574-6968.1995.tb07492.x.
Human immunoglobulin G Fc fragment-binding activity of Mycoplasma salivarium cells was remarkably enhanced by trypsin treatment of the cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile of proteins of the cells treated with trypsin was the same as that of the cells treated with pronase, although pronase treatment had been shown to reduce the activity in our previous study (FEMS Microbiol. Lett. 123, 305-310, 1994). This contradiction was clarified by the finding that trypsin bound the Fc fragment more strongly than the cells, and a small amount of trypsin remained in the cells treated with trypsin and washed well. On the basis of these results, it was concluded that the enhancement of cell activity by trypsin treatment was ascribed to binding of the Fc fragment to trypsin remaining in the trypsin-treated cells.
唾液支原体细胞经胰蛋白酶处理后，其与人免疫球蛋白G Fc片段的结合活性显著增强。经胰蛋白酶处理的细胞蛋白质的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳图谱与经链霉蛋白酶处理的细胞相同，尽管在我们之前的研究（《FEMS微生物学快报》123，305 - 310，1994）中已表明链霉蛋白酶处理会降低活性。通过发现胰蛋白酶比细胞更强烈地结合Fc片段，以及在用胰蛋白酶处理并充分洗涤的细胞中仍残留少量胰蛋白酶，这一矛盾得以阐明。基于这些结果，得出结论：胰蛋白酶处理导致细胞活性增强归因于Fc片段与残留在经胰蛋白酶处理细胞中的胰蛋白酶结合。
