Surface plasmon resonance imaging of limited glycoprotein samples

Surface plasmon resonance imaging of limited glycoprotein samples
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有限糖蛋白样品的表面等离子共振成像

DOI:
10.1039/b804235g
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发表时间:
2008-09-01
期刊:
影响因子:
4.2
通讯作者:
Yan, Mingdi
Yan, Mingdi
中科院分区:
化学2区
文献类型:
--
作者:
Liu, Wei;Chen, Yi;Yan, Mingdi

文献摘要

被引文献

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一种表面等离子体共振成像方法已被开发用于低水平糖蛋白的高通量识别和测定,具有至少低至50 nL的有限样品体积。以鸡卵清蛋白和免疫球蛋白G为模型化合物,以牛血清白蛋白和溶菌酶为对照。将浓度为0.0080-1.0 mg mL(-1)的每种蛋白质印刷在一个金传感膜上,同时将膜与探针溶液反应,并使用实验室构建的表面等离子体共振成像系统进行观察。成像信号依赖于分析物的浓度和类型,检测限低至至少0.5 ng。通过与200 nM伴刀豆球蛋白A(con A)反应,可以很容易地将1.0 mg mL(-1)或0.010 mg mL(-1)的糖蛋白与非糖蛋白区分开来,识别极限也低至0.5 ng糖蛋白。因此,这种成像方法被认为是分析糖蛋白的新工具。
A surface plasmon resonance imaging method has been developed for high throughput recognition and determination of low level glycoproteins with limited sample volume at least down to 50 nL. Chicken ovalbumin and immunoglobulin G were chosen as model compounds while bovine serum albumin and lysozyme were used as control. Each protein, at a concentration of 0.0080-1.0 mg mL(-1), was printed on one gold sensing film, and the films were simultaneously reacted with a probe solution and viewed using a laboratory-built surface plasmon resonance imaging system. The imaging signals were dependent on the concentration and the type of analyte, with a limit of detection down to at least 0.5 ng. The glycoproteins dotted at either 1.0 mg mL(-1) or 0.010 mg mL(-1) were easily differentiated from the non-glycoproteins by reaction with 200 nM concanavalin A (con A), giving a limit of recognition down also to 0.5 ng glycoprotein. This imaging method was hence considered a new tool for analyzing glycoproteins.