Spherical aggregates of lead phosphate hydroxyapatite (PbHA) have been
developed as an adsorbent in high-performance liquid chromatography.
There are effectively two types of crystal surface, a (or b) and c whi
ch appear on the crystal, analogous to the case of calcium phosphate h
ydroxyapatite. Basic proteins adsorb to the c surface, and can be elut
ed by chloride or phosphate salts. Acidic proteins adsorb to the a (or
b) surface, and are eluted only by phosphate. All proteins were adsor
bed at pH 6 and eluted at pH 8-10. The binding capacity of PbHA for bo
vine serum albumin was determined by frontal analysis; the shape of th
e adsorption isotherm is of the Langmuir type.