Wassell D T, Hall R C, Embery G
Department of Basic Dental Science, Cardiff Dental School, University of Wales College of Medicine, Health Park, UK.
Biomaterials. 1995 Jun;16(9):697-702. doi: 10.1016/0142-9612(95)99697-k.
The adsorption of bovine serum albumin (BSA) onto hydroxyapatite (HA) has been studied as a function of protein concentration, pH and ionic strength. Isotherm data (adsorption being a reversible process) have been analysed using the Langmuir model, the adsorption parameters AT (maximum amount of protein adsorbed, mg m-2) and K (affinity constant, L g-1) being calculated for each solution condition (except NaF). For the pH dependence of adsorption, both AT and K increase with decreasing pH, indicating that both electrostatic and hydration effects are important. For the ionic strength dependence, increasing NaCI concentrations result in a slight increase in AT, but K decreases. With increasing CaCI2 concentrations the AT and K values increase, the opposite being true for increasing concentrations of Na2HPO4. NaF both enhances and inhibits adsorption depending on the concentration. Possible reasons for these results are discussed.
已研究了牛血清白蛋白（BSA）在羟基磷灰石（HA）上的吸附情况，该吸附是蛋白质浓度、pH值和离子强度的函数。等温线数据（吸附为可逆过程）已使用朗缪尔模型进行分析，针对每种溶液条件（除NaF外）计算了吸附参数AT（最大吸附蛋白量，mg m-2）和K（亲和常数，L g-1）。对于吸附的pH依赖性，AT和K均随pH降低而增加，表明静电和水合作用都很重要。对于离子强度依赖性，NaCl浓度增加导致AT略有增加，但K降低。随着CaCl2浓度增加，AT和K值增加，而随着Na2HPO4浓度增加情况则相反。NaF根据浓度既增强又抑制吸附。讨论了这些结果的可能原因。
