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INTERACTION OF CELLULOSE WITH PROTEINS

机译:纤维素与蛋白质的相互作用

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摘要

Adsorption of human serum albumin (HSA) to mi-crocrystalline cellulose (MCC) interface has been determined as functions of protein concentration and pH of the aqueous medium. The maximum adsorption value is reached at the HSA isoelectric point The isotherms with respect to the adsorption of HSA are S-shaped in character. The study of adsorption at several values of pH of the medium indicates that interaction of HSA with the MCC interface is not controlled by the electrostatic effect. The desorption data reveal that HSA is strongly bound to the MCC matrix.
机译:已确定人血清白蛋白(HSA)对微晶纤维素(MCC)界面的吸附是蛋白质浓度和水性介质pH的函数。在HSA等电点达到最大吸附值。关于HSA吸附的等温线为S形。对在几种pH值的介质上吸附的研究表明,HSA与MCC界面的相互作用不受静电作用的控制。解吸数据表明HSA与MCC基质牢固结合。

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