Inhibitory effect of serum globulins on the adhesion of Prevotella nigrescens to hydroxyapatite.

Prevotella nigrescens ATCC 25261 cells adhere well to protein-blocking hydroxyapatite (HA) which mimics a root surface in the periodontal pocket treated with proteases such as trypsin, proteinase K, chymotrypsin and papain. This study was done to clarify the inhibitory effect of alpha- and beta- serum globulins on the adhesion of P. nigrescens ATCC 25261 cells to trypsin-treated HA. The inhibitory effect was found to be caused by the alpha1-antitrypsin (alpha1-AT) of alpha-globulin and the low-density lipoprotein (LDL) of beta-globulin under experimental conditions. The most effective inhibition of alpha1-AT on P. nigrescens ATCC 25261 cell attachment to HA was achieved when alpha1-AT-treated trypsin was used. The most effective inhibition of LDL occurred when trypsin-treated HA was treated with LDL. Apo-transferrin (TF) and holo-TF, which are beta-globulins, did not affect the attachment of P. nigrescens ATCC 25261 cells to trypsin-treated HA.