Lectin-based affinity capture for MALDI-MS analysis of bacteria
Lectin-based affinity capture for MALDI-MS analysis of bacteria
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DOI：
10.1021/ac981119h
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发表时间：
1999-04-01
影响因子：
7.4
通讯作者：
Fenselau, C
中科院分区：
文献类型：
--
作者：
Bundy, J;Fenselau, C
固定化凝集素现已被纳入亲和表面，可用于分离大类样品进行质谱分析。从含有盐、尿素、缓冲液和其他对MALDI质谱有害的污染物的溶液中分离并浓缩碳水化合物和显示碳水化合物结合基序的细菌物种。通过自组装单层将伴刀豆球蛋白A固定到金箔上。将磷酸盐缓冲液或尿液中的样品施加到捕获表面并允许相互作用。然后洗涤捕获表面以除去盐和其他未结合的组分，并在飞行时间质谱仪上进行基质辅助激光解吸/电离。凝集素衍生的表面允许样品被浓缩，并容易在相对低的水平进行表征。
Immobilized lectins have now been incorporated into affinity surfaces that can be used to isolate broad classes of samples for mass spectrometric analysis. A carbohydrate and a bacterial species that displays the carbohydrate binding motif were isolated and concentrated out of solutions containing salt, urea, buffers, and other contaminants that are deleterious to MALDI mass spectrometry, Concanavalin A was immobilized to a gold foil via a self-assembled monolayer. Samples in phosphate buffer or urine were applied to the capture surface and allowed to interact. The capture surface was then washed to remove salts and other unbound components and subjected to matrix-assisted laser desorption/ionization on a time-of-flight mass spectrometer. The lectin-derivatized surface allowed samples to be concentrated and readily characterized at relatively low levels.