SURFACE CONTROL OF CATTLE BONE-ORIGINATED APATITES FOR ADSORPTION OF DIFFERENT PROTEINS BY HEAT-TREATMENTS
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- YOSHIDA MASASHI
- Department of Chemical System Engineering, Kitami Institute of Technology
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- AKAZAWA TOSHIYUKI
- Hokkaido Industrial Research Institute
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- KOBAYASHI MASAYOSHI
- Department of Chemical System Engineering, Kitami Institute of Technology
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- SUGIMURA HIROMI
- Department of Chemical System Engineering, Kitami Institute of Technology
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- KANNO TOHRU
- Department of Chemical System Engineering, Kitami Institute of Technology
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- HORIUCHI JUNICHI
- Department of Chemical System Engineering, Kitami Institute of Technology
Abstract
Cattle bone-originated apatites (r-HAp) powders were prepared by a dissolution-precipitation and subsequent heat-treatments at 673~1073 K. Adsorption characteristics on the r-HAp powders were investigated for different proteins such as bovine serum albumin (BSA), myoglobin from horse skeletal muscle (MOG), ribonuclease A from bovine pancreas (RBN), lysozyme from chicken egg white (LSZ), and cytochrome c from horse heart (CTC). The adsorption for each of the proteins obeyed the Langmuir equation. The saturated amounts of LSZ, CTC, and RBN (basic proteins with isoelectric points (E0) > 7.0) adsorbed (ASB) were 2~10 times larger than those of BSA and MOG (acidic proteins with E0 < 7.0) adsorbed (ASA). As the heat-treatment temperature was elevated, the ASB and ASA gradually increased, and the ratios of ASB to ASA decreased, and heats of adsorption for basic proteins increased, whereas those for acidic proteins decreased. These characteristic changes can contribute to a design of liquid chromatographic column for adsorption-separation of the proteins.
Journal
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- Phosphorus Research Bulletin
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Phosphorus Research Bulletin 10 (0), 359-363, 1999
Japanese Association of Inorganic Phosphorus Chemistry
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Details 詳細情報について
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- CRID
- 1390282680439507456
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- NII Article ID
- 130004992353
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- COI
- 1:CAS:528:DC%2BD3cXmtlOqtb4%3D
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- ISSN
- 09184783
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- Text Lang
- en
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed