The adsorption of lysozyme (LSZ) onto various kinds of synthetic hydro
xyapatite (X-10(PO4)(6)(OH)(2), denoted as CaHAP, SrHAP, and CaSrHAP f
or X = Ca, Sr, and Ca + Sr, respectively) particles was investigated a
t 15 degrees C in a 1 x 10(-4) mol dm(-3) KCI solution of pH 6.0. The
adsorption isotherms of LSZ onto these HAPs exhibited the pseudo-langm
uir type as well as those of bovine serum albumin (BSA). The negative
electrophoretic mobility of the particles was reversed to a positive o
ne by adsorption of positively charged LSZ molecules. No remarkable re
lationship between saturated amounts of adsorbed LSZ (n(s)) and the ca
tion/P molar ratio of the particles was observed on CaHAP systems, In
the case of SrHAP and CaSrHAP, however, n(s) approached zero at a cati
on/P molar ratio of ca. 1.70. The n(s) values of LSZ on CaHAP, SrHAP,
and CaSrHAP particles are appreciably smaller than those of BSA. This
study provides the first conclusive evidence that LSZ molecules specif
ically adsorb onto phosphate ions on ac or be faces and/or on negative
ly charged sites formed by six oxygen atoms of three phosphate ions on
ab crystal faces (P sites) on the HAP surface by using basic amino gr
oups, though the low probability of the latter mode was insinuated. (C
) 1997 Academic Press.