Pitt W G, Cooper S L
Department of Chemical Engineering, University of Wisconsin, Madison 53706.
J Biomed Mater Res. 1988 May;22(5):359-82. doi: 10.1002/jbm.820220502.
The initial adsorption rate of delipidized Human Serum Albumin (HSA) is increased by addition of C-18 alkyl chains to a polyurethane. The presence of alkyl chains does not appear to influence the total amount of HSA adsorbed after one hour exposure to a 5.0 mg/mL HSA solution. Neither does the desorption following one hour of adsorption appear to be influenced by the presence of alkyl chains. A study of the effects of solution concentration and temperature showed that the initial adsorption rates on both polymers are proportional to the protein concentration raised to the 0.36 power, and that alkylation of the polymer increases the activation energy of the initial adsorption rate above the 14 kJ/mol observed for the underivatized polyurethane. A new technique is presented to quantify the mass of adsorbed protein using Fourier transform infrared spectroscopy and attenuated total reflection optics. This technique uses the absorbance of bulk protein as an internal calibration reference, and appears to be as accurate and perhaps more precise than radiolabeling techniques.
通过向聚氨酯中添加C-18烷基链，脱脂人血清白蛋白（HSA）的初始吸附速率得以提高。烷基链的存在似乎并不影响在5.0 mg/mL HSA溶液中暴露一小时后吸附的HSA总量。吸附一小时后的解吸也似乎不受烷基链存在的影响。对溶液浓度和温度影响的研究表明，两种聚合物上的初始吸附速率均与蛋白质浓度的0.36次方成正比，并且聚合物的烷基化使初始吸附速率的活化能高于未衍生化聚氨酯所观察到的14 kJ/mol。提出了一种使用傅里叶变换红外光谱和衰减全反射光学器件来量化吸附蛋白质质量的新技术。该技术使用大量蛋白质的吸光度作为内部校准参考，并且似乎与放射性标记技术一样准确，甚至可能更精确。
