Adsorption Studies of Enzymes and Other Proteins

Zittle, Charles A.

doi:10.1002/9780470122594.ch9

Cited by 21 publications

(3 citation statements)

References 208 publications

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“…Porous HAp ceramics have been used as hard tissue‐repairing materials in clinics. Since Zittle et al reported protein adsorption onto calcium phosphates in 1951, 1 HAp has been used as a column packing material for chromatography to separate proteins or enzymes 2–4 . In addition, much attention has been focused on HAp as an adsorbent for removing pathogenic proteins from blood in blood purification therapy.…”

Section: Introductionmentioning

confidence: 99%

Structural Characterization and Protein Adsorption Property of Hydroxyapatite Particles Modified With Zinc Ions

Hayakawa

Ando

Tsuru

et al. 2007

Journal of the American Ceramic Society

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Zinc-containing hydroxyapatite particles (Zn/HAp) were prepared by an ion exchange reaction process involving hydroxyapatite (HAp) particles with aqueous solutions containing various amounts of zinc nitrate. The Zn 21 ion was partially substituted for the Ca 21 ion position in the HAp lattice, and hence, the obtained samples had changed little in crystallinity, particle size, and specific surface area. Adsorption of bovine serum albumin (BSA) and b 2 -microglobulin (b 2 -MG) in solutions containing both BSA and b 2 -MG was examined. As the Zn 21 ion content in the apatites increased, the adsorbed amount of BSA was almost constant, whereas that of b 2 -MG increased.

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Section: Introductionmentioning

confidence: 99%

Structural Characterization and Protein Adsorption Property of Hydroxyapatite Particles Modified With Zinc Ions

Hayakawa

Ando

Tsuru

et al. 2007

Journal of the American Ceramic Society

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“…Hydroxyapatite has been used both as a bone‐substitute material and as a column packing material for chromatography to separate proteins or enzymes 1–4. Zittle reported protein adsorption onto calcium phosphates1 in 1951. Since then, extensive studies have been conducted on the mechanisms of protein adsorption 5–8.…”

Section: Introductionmentioning

confidence: 99%

Selective protein adsorption and blood compatibility of hydroxy‐carbonate apatites

Takemoto

Kusudo

Tsuru

et al. 2004

J Biomedical Materials Res

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We examined the blood compatibility and protein adsorption on hydroxyapatite and hydroxy-carbonate apatite. Those apatites were synthesized under a 0, 5, or 15% CO(2)-containing N(2) atmosphere by a wet-chemical method with a strong ammonia alkali solution of calcium nitrate and diammonium hydrogen phosphate (5:3 in molar ratio) and subsequent calcination in the range of 105-700 degrees C. From infrared (IR) analysis, the carbonate ions substituted both phosphate ions and hydroxyl ions in the hydroxyapatite lattice; the intensities of IR bands assignable to phosphate ions and hydroxyl ions were reduced on calcinations. The specific surface areas of synthesized apatites decreased with increasing calcination temperature. Blood-clotting properties were evaluated in terms of active partial thromboplastin time, prothrombin time, and the amount of fibrinogen for the plasma in contact with the apatites, indicating that all the apatites barely influenced the blood clotting system. The apatites were in contact with a solution containing both bovine serum albumin (BSA) and beta(2)-microglobulin (beta(2)-MG), and the amounts of those proteins adsorbed on them were examined: the amount of absorbed BSA and beta(2)-MG gradually increased with the calcination temperature below 500 degrees C, while it showed a sudden increase when more than 600 degrees C. Hydroxy-carbonate apatite synthesized under a 15% CO(2)-containing N(2) atmosphere and calcined below 400 degrees C had the greatest selectivity in adsorbing beta(2)-MG. Thus, a higher selectivity for beta(2)-MG adsorption was empirically correlated to carbonate ions incorporated in the hydroxyapatite lattice.

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“…It is well known that proteins can adsorb to various solid surfaces through hydrophobic, electrostatic or other interactions [1][2][3][4][5][6]. Indeed, proteins with a low internal stability, such as BSA, can adsorb on all surfaces owing to a gain in conformational entropy resulting from adsorption [7].…”

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confidence: 99%

Avoiding adsorption of Bcl-2 proteins to plasticware is important for accurate quantitation

et al. 2019

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Adsorption Studies of Enzymes and Other Proteins

Cited by 21 publications

References 208 publications

Structural Characterization and Protein Adsorption Property of Hydroxyapatite Particles Modified With Zinc Ions

Structural Characterization and Protein Adsorption Property of Hydroxyapatite Particles Modified With Zinc Ions

Selective protein adsorption and blood compatibility of hydroxy‐carbonate apatites

Avoiding adsorption of Bcl-2 proteins to plasticware is important for accurate quantitation

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