多种蛋白质固定相：综述
Multiple protein stationary phases: a review.
作者信息
Singh N S, Habicht K-L, Dossou K S S, Shimmo R, Wainer I W, Moaddel R
机构信息
Biomedical Research Center, National Institute on Aging, National Institutes of Health, 251 Bayview Boulevard, Suite 100, Baltimore, MD 21224, USA.
Department of Natural Sciences, Institute of Mathematics and Natural Sciences, Tallinn University, Narva mnt. 29, 10120 Tallinn, Estonia.
出版信息
J Chromatogr B Analyt Technol Biomed Life Sci. 2014 Oct 1;968:64-8. doi: 10.1016/j.jchromb.2014.04.005. Epub 2014 Apr 13.
Abstract
Cellular membrane affinity chromatography stationary phases have been extensively used to characterize immobilized proteins and provide a direct measurement of multiple binding sites, including orthosteric and allosteric sites. This review will address the utilization of immobilized cellular and tissue fragments to characterize multiple transmembrane proteins co-immobilized onto a stationary phase. This approach will be illustrated by demonstrating that multiple transmembrane proteins were immobilized from cell lines and tissue fragments. In addition, the immobilization of individual compartments/organelles within a cell will be discussed and the changes in the proteins binding/kinetics based on their location.
摘要
细胞膜亲和色谱固定相已被广泛用于表征固定化蛋白质，并直接测量多个结合位点，包括正构位点和变构位点。本综述将探讨利用固定化细胞和组织片段来表征共固定在固定相上的多个跨膜蛋白。通过展示从细胞系和组织片段中固定多个跨膜蛋白来说明这种方法。此外，还将讨论细胞内单个区室/细胞器的固定化以及基于其位置的蛋白质结合/动力学变化。
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