The enhancement of the human immunoglobulin G Fc fragment-binding activity of Mycoplasma salivarium cells by trypsin treatment is ascribed to the binding of trypsin to the Fc fragment.
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.
Sawa
Y
Y
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Japan.
Shibata
K
K
Watanabe
T
T
D007141:Immunoglobulin Fc Fragments / Q000187:drug effects / Q000378:metabolism*; D007074:Immunoglobulin G / Q000378:metabolism*; D009174:Mycoplasma / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D014357:Trypsin / Q000378:metabolism* / Q000494:pharmacology*
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D014357:Trypsin