Properties of cattle bone powder-coated composite particles as high-performance and open column liquid chromatographic column packings

• Published in: Journal of Chromatography A Vol. 813; no. 1; pp. 21 - 33
• Main Authors: Honda, Futaba, Honda, Hirotaka, Koishi, Masumi, Matsuno, Takashi
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 10.07.1998; Elsevier
• Subjects: Adsorption; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Bone and Bones - chemistry; Cattle; Chromatography, High Pressure Liquid - instrumentation; Chromatography, High Pressure Liquid - methods; Durapatite; Fundamental and applied biological sciences. Psychology; gamma-Globulins; General aspects, investigation methods; Hydrogen-Ion Concentration; Hydroxyapatite; Indicators and Reagents; Microscopy, Electron, Scanning; Polyethylenes; Powders; Proteins; Spectrophotometry, Ultraviolet; X-Ray Diffraction; Proteins; Cattle bone powder; Hydroxyapatite; Stationary phases, LC; Chromatographic retention; Adsorption capacity; HPLC chromatography; Composite material; Powder; Surface structure; Adsorbent; Ungulata; Stationary phase; Scanning electron microscopy; Polyethylene; Bovine; Enzyme; Glycoproteins; Serum albumin; Globulin γ; Experimental study; Serum protein; Vertebrata; Mammalia; Ultraviolet detector; Animal; Morphology; Preparation; Artiodactyla; Bone; Surface area; Packed column
• ISSN: 0021-9673
• DOI: 10.1016/S0021-9673(98)00336-7

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.