Improved liquid chromatographic separation of different proteins by designing functional surfaces of cattle bone-originated apatite.
Spherical particles of cattle bone-originated hydroxyapatite (r-HAp) were prepared by dissolution-precipitation, spray-drying using a two fluid-nozzle apparatus, and subsequent heat treatment. The product had effective pore structures for liquid chromatographic separation of albumin, myoglobin, ribonuclease, lysozyme and cytochrome c. The activated surfaces of the r-HAp particles were easily prepared with desired proportions of P- and C-sites and appropriate acid-basic strength for selective protein adsorption by optimizing the synthesis conditions. Liquid chromatography columns packed with the particles exhibited high resolution and durability in protein separation, reflecting stable distribution of pore size.
Akazawa
T
T
Hokkaido Industrial Research Institute, Sapporo, Japan. akazawa@hokkaido-iri.go.jp
Kobayashi
M
M
Yoshida
M
M
Matsushima
K
K
Minoshima
H
H
Sugimura
H
H
Kanno
T
T
Horiuchi
J
J
D000818:Animals; D001672:Biocompatible Materials / Q000032:analysis*; D001842:Bone and Bones / Q000737:chemistry*; D002417:Cattle; D002853:Chromatography, Liquid; D017886:Durapatite / Q000032:analysis*; D005269:Femur / Q000737:chemistry; D008863:Microspheres; D016062:Porosity; D011506:Proteins / Q000737:chemistry*
D001672:Biocompatible Materials; D011506:Proteins; D017886:Durapatite