S. Fujimura et al., SOME BINDING-PROPERTIES OF THE ENVELOPE OF PORPHYROMONAS-GINGIVALIS TO HEMOGLOBIN, FEMS immunology and medical microbiology, 10(2), 1995, pp. 109-114
Porphyromonas gingivalis was found to bind to hemoproteins (hemoglobin
, myoglobin, catalase, cytochrome c) and the binding properties of the
envelope of P. gingivalis to hemoglobin were investigated. Maximum am
ount of hemoglobin bound to 1 mg of the envelope was 58 mu g. No signi
ficant binding was observed at 4 degrees C and the binding was inhibit
ed strongly by tosyl-L-lysine chloromethyl ketone, Leupeptin, EDTA and
partially by meta-periodate. Heating of the envelope at 70 degrees C
for 15 min resulted in complete lass of the binding activity. The bind
ing activity of the envelope was not influenced by the treatment with
the endogenous proteases. The envelope saturated with hemoglobin could
no longer bind to other hemoproteins tested, indicating that binding
site for these hemoproteins are common.