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Protein-imprinted soft-wet gel composite microspheres with magnetic susceptibility. II. Characteristics

机译:具有磁化率的蛋白质印迹软湿凝胶复合微球。二。特点

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Protein-imprinted soft-gel composite microspheres with magnetic susceptibility (MS-PIGMs) were prepared by inverse suspension polymerization using Fe3O4 particles as magnetically susceptible component and bovine serum albumin and lysozyme (Lyz) as templates, respectively. The average content of magnetically susceptible component (Fe3O4) inside MS-PIGMs was determined using thermogravimetric analyzer, and the magnetic characteristics of MS-PIGMs were measured by vibrating sample magnetometer. The results showed that the resulting MS-PIGMs had a certain magnetic response to external magnetic fields, and their average content of Fe3O4 was 2.08%. Their recognition specificity was investigated using BSA and Lyz as both templates and control molecules and characterized by high-performance liquid chromatography, and the mechanism of imprinting and recognition was analyzed. It was shown that the resulting BSA imprinted soft-gel composite microspheres with magnetic susceptibility (BSA-PIGMs) and Lyz imprinted soft-gel composite microspheres with magnetic susceptibility (Lyz-PIGMs). All exhibited good recognition selectivity for their templates, and the relative separation factor (beta) was 4.75 and 5.88, respectively. The recognition selectivity of MS-PIGMs to their templates depended mainly on the synergic action of a large quantity of hydrogen binding being caused by complementation and very close contact of outer surface of proteins with inner surface of "imprinting cavities." (c) 2005 Wiley Periodicals, Inc.
机译:以Fe3O4颗粒为磁敏组分,以牛血清白蛋白和溶菌酶(Lyz)为模板,通过反相悬浮聚合制备具有磁化率的蛋白质印迹软凝胶复合微球(MS-PIGMs)。使用热重分析仪测定MS-PIGMs内部磁敏组分(Fe3O4)的平均含量,并通过振动样品磁力计测量MS-PIGMs的磁特性。结果表明,生成的MS-PIGMs对外部磁场具有一定的磁响应,其平均Fe3O4含量为2.08%。以BSA和Lyz为模板和对照分子对它们的识别特异性进行了研究,并通过高效液相色谱进行了表征,并分析了印迹和识别的机理。结果表明,所得的BSA印迹具有磁化率的软凝胶复合微球(BSA-PIGMs)和Lyz印迹具有磁化率的软凝胶复合微球(Lyz-PIGMs)。所有人都对其模板表现出良好的识别选择性,相对分离系数(β)分别为4.75和5.88。 MS-PIGM对模板的识别选择性主要取决于大量的氢键的协同作用,这种相互作用是由于蛋白质的外表面与“印迹腔”的内表面互补和非常紧密的接触而引起的。 (c)2005年Wiley Periodicals,Inc.

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