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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:已经确定了人血清白蛋白(HSA)至MI-克罗克纤维素(MCC)界面的吸附作为蛋白质浓度和水性介质的pH的函数。在HSA等电点达到最大吸附值,在相对于HSA吸附的等温物质是特征的S形。在培养基的几个pH值下吸附的研究表明,HSA与MCC界面的相互作用不受静电效应控制。解吸数据揭示了HSA强烈地绑定到MCC矩阵。

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