Abstract
An adsorption of proteins on the needle-like hydroxyapatite (N-HAp) after heat treatment at 100-700°C was investigated. Adsorbed amount of Bovine Serum Arubumine (BSA) as an acidic protein decreased with increasing heat treatment temperature except 700°C, whereas that for Lysozyme chloride (LYZ) as a basic protein increased with treatment temperature. Colloidal vibration potentials (CVP) of all N-HAps showed negative potentials in a phosphate buffer solution at pH6.8, and shifted to more negative regions with increasing treatment temperature. Based on the XRD patterns, the N-HAps treated at 100-400°C were HAp phase only, but β-TCP (Ca3(PO4)2) phase appeared in the N-HAp treated at 700°C.
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