Delineating protein-protein interactions via biomolecular interaction analysis-mass spectrometry.
Delineating protein-protein interactions via biomolecular interaction analysis-mass spectrometry.
复制标题
通过生物分子相互作用分析-质谱法描述蛋白质-蛋白质相互作用。
DOI：
10.1002/jmr.600
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Nelson,RandallW
中科院分区：
文献类型：
--
作者：
Nedelkov,Dobrin;Nelson,RandallW
The utility of biomolecular interaction analysis–mass spectrometry (BIA/MS) in screening for protein–protein interactions was explored in this work. Experiments were performed in which proteins served as ligands for screening of possible interactions with other proteins from human plasma and urine. The proteins utilized were beta‐2‐microglobulin, cystatin C (cysC), retinol binding protein (RBP), transthyretin (TTR), alpha‐1‐microglobulin, C‐reactive protein, transferrin and papain. The immobilization of functionally active proteins was confirmed via interactions with antibodies to the corresponding proteins. Various dilutions of human urine and plasma were injected over the protein‐derivatized surfaces. It was observed that the urine injections generally yielded smaller SPR responses than those observed after the plasma injections. The BIA/MS experiments did not reveal novel protein–protein interactions, although several established interactions (such as those between RBP and TTR, and cysC and papain) were validated. Few protein ligand deficiencies (such as truncations) leading to false negative and false positive BIA/MS results were also discovered. Copyright © 2003 John Wiley & Sons, Ltd.
