Inactivation of the vascular permeability-increasing activity of bradykinin by mycoplasmas.
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 degrees C for 1 h. Cell components responsible for inactivation of the activity of bradykinin were found to be arginine-specific aminopeptidase and carboxypeptidase.
Shibata
K
K
Department of Oral Bacteriology, Nagasaki University School of Dentistry, Japan.
Watanabe
T
T
D000128:Acholeplasma laidlawii / Q000201:enzymology / Q000502:physiology; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D001920:Bradykinin / Q000037:antagonists & inhibitors*; D002199:Capillary Permeability; D002855:Chromatography, Thin Layer; D006651:Histocytochemistry; D001121:Lysine Carboxypeptidase / Q000378:metabolism; D008297:Male; D009174:Mycoplasma / Q000201:enzymology / Q000502:physiology*; D009177:Mycoplasma pneumoniae / Q000201:enzymology / Q000502:physiology; D011817:Rabbits; D014509:Ureaplasma / Q000201:enzymology / Q000502:physiology
D000626:Aminopeptidases; C019721:aminopeptidase B; D001121:Lysine Carboxypeptidase; D001920:Bradykinin