A versatile method of identifying specific binding proteins on affinity resins.
The isolation of both specific and nonspecific binding proteins on affinity matrices bearing bioactive compounds hinders the identification of drug cellular targets. Although solid-phase elution and competition methods conventionally are used to distinguish between specific and nonspecific receptor-ligand interactions, these approaches often are severely restricted by low ligand solubility and/or slow kinetic dissociation. This article describes an alternative and versatile method, termed serial affinity chromatography, to identify ligand receptors using affinity resins.
Department of Chemistry, Reverse Proteomics Research Institute, 2-6-7 Kazusa-Kamatari, Chiba 292-0818, Japan.
Kiyoshi
K
Yamamoto
Akira
A
Yamazaki
Mikio
M
Takeuchi
Akito
A
Tanaka
D000345:Affinity Labels / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000166:cytology / Q000378:metabolism; D002352:Carrier Proteins / Q000032:analysis* / Q000737:chemistry / Q000302:isolation & purification*; D002478:Cells, Cultured; D002846:Chromatography, Affinity / Q000379:methods*; D006801:Humans; D008024:Ligands; D008954:Models, Biological; D051381:Rats; D012117:Resins, Synthetic / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D022061:Tacrolimus Binding Protein 1A / Q000302:isolation & purification
D000345:Affinity Labels; D002352:Carrier Proteins; D008024:Ligands; D012117:Resins, Synthetic; D022061:Tacrolimus Binding Protein 1A