Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1377678 | Bioorganic & Medicinal Chemistry Letters | 2006 | 4 Pages |
Abstract
Poly(methacrylate) matrices for affinity resins were designed and synthesized based on our previous results that nonspecific protein absorption on affinity resins strongly depended on their hydrophobic property. The novel affinity resins bearing FK506 (6a, 6b) captured specific binding protein, FKBP12, with a small amount of nonspecific binding proteins. The amount of nonspecific binding proteins on 6a-6b was much reduced compared to that on commercially available poly(methacrylate) resins, Toyopearl⢠(8), and was almost the same as that on one of the most popular resins, Affigel⢠(9). Interestingly, 6a and 6b could isolate FKBP52 as a specific binding protein as well, although 8 and 9 could not.
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Authors
Teruki Takahashi, Takaaki Shiyama, Ken Hosoya, Akito Tanaka,