Adsorption of myoglobin onto various synthetic hydroxyapatite particles
Adsorption of myoglobin onto various synthetic hydroxyapatite particles
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DOI：
10.1039/a909396f
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发表时间：
2000-01-01
影响因子：
3.3
通讯作者：
Ishikawa, T
中科院分区：
文献类型：
--
作者：
Kandori, K;Fudo, A;Ishikawa, T
在15 ℃、1 × 10 ~（-4）mol dm ~（-3）KCl溶液中，研究了不同种类的胶体合成羟基磷灰石[X-10（PO_4）（6）（OH）（2），X=Ca、Sr和Ca+Sr时分别记为CaHap、SrHap和CaSrHap]颗粒对肌红蛋白（MGB）的吸附。CaHap对MGB的吸附速率与溶菌酶（LSZ）相当，且比牛血清白蛋白（BSA）快。这种区别是由这些蛋白质（MGB：17 800 Da，LSZ：14 600 Da，BSA：67 200 Da）的分子量的差异解释;较小的MGB和LSZ分子的CaHap表面的扩散速率比较大的BSA更快。这些合成羟基磷灰石（Haps）上的吸附等温线的MGB表现出的Langmuir型和MGB覆盖的Haps的表面电荷显示几乎恒定的负值，是独立的MGB的浓度为所有的Haps。的饱和量的吸附的MGB的CaHap的值是独立的Ca：PO 4的摩尔比的材料，支持不太重要的MGB和Haps之间的静电相互作用，因为MGB分子在pH值为6的静电中性。据推测，MGB分子被吸附到暴露在ac和bc晶面上的磷酸根离子上的货车德瓦尔斯吸引力，而不利用静电相互作用。
The adsorption of myoglobin (MGB) onto various kinds of colloidal synthetic hydroxyapatite [X-10(PO4)(6)(OH)(2), noted CaHap, SrHap and CaSrHap for X=Ca, Sr and Ca+Sr, respectively] particles was investigated at 15 degrees C in a 1x10(-4) mol dm(-3) KCl solution of pH 6.0. The adsorption rate of MGB onto CaHap was comparable to that of lysozyme (LSZ) and was faster than that of bovine serum albumin (BSA). This distinction was explained by the difference in the molecular mass of these proteins (MGB: 17 800 Da, LSZ: 14 600 Da, BSA: 67 200 Da); the diffusion rates of the smaller MGB and LSZ molecules to the CaHap surface are faster than that of the larger BSA. The adsorption isotherms of MGB onto these synthetic hydroxyapatites (Haps) exhibited the Langmuir type and the surface charge of the MGB-covered Haps showed almost constant negative value and was independent of the MGB concentration for all the Haps. The values of the saturated amounts of adsorbed MGB for CaHap were independent of the Ca:PO4 molar ratio of the materials, supporting less importance of an electrostatic interaction between MGB and Haps because MGB molecules are electrostatically neutral at pH 6. It was presumed that MGB molecules are adsorbed onto phosphate ions exposed on ac and bc crystal faces by the van der Waals attractive force without taking advantage of the electrostatic interaction.