Abstract
Cattle bone powder (CBP) from natural resources was employed as a protein adsorbent instead of chemically synthesized hydroxyapatite (HA). Though a small amount of impurities was detected, CBP possessed a crystallinity similar to HA. Using CBP/40PE prepared from CBP and polyethylene beads (40 μm) by dry impact blending as an HPLC column packing, considerable correlation was observed between the elution concentrations of proteins and their p I. Such behavior was caused by the relatively large adsorption capacity for basic proteins. CBP/40PE could completely separate γ-globulin from BSA also as an open column chromatographic support, under relatively low concentration.
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