Open AccessInactivation of the vascular permeability‐increasing activity of bradykinin by mycoplasmas
Author(s) -
Shibata Kenichiro,
Watanabe Tsuguo
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03613.x
Subject(s) - bradykinin , carboxypeptidase , incubation , microbiology and biotechnology , mycoplasma pneumoniae , ureaplasma urealyticum , chemistry , mycoplasma genitalium , arginine , mycoplasmataceae , mycoplasma , aminopeptidase , mycoplasma hominis , mollicutes , enzyme , biology , biochemistry , immunology , amino acid , medicine , leucine , receptor , chlamydia trachomatis , pneumonia
Mycoplasma pneumoniae, M. genitalium, M. fermentans, M. hominis, M. salivarium, M. orale, Ureaplasma urealyticum and Acholeplasma laidlawii inactivated the vascular permeability‐increasing activity of bradykinin when the mixture of bradykinin and mycoplasma cells was injected after incubation at 37°C for 1 h. Cell components responsible for inactivation of the activity of bradykinin were found to be arginine‐specific aminopeptidase and carboxypeptidase.