The binding of cupric ions to bovine serum albumin was investigated by using a cupric-ion-specific electrode. When using a modified form of the Scatchard equation, it was determined that there are at least two classes of binding sites on bovine serum albumin for cupric ions. One class has three bind
Cupric ion enhanced molecular imprinting of bovine serum albumin in hydrogel
✍ Scribed by Sheng-Hua Li; Jun Wang; Mei-Ping Zhao
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 511 KB
- Volume
- 32
- Category
- Article
- ISSN
- 1615-9306
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
A novel molecularly imprinted hydrogel for bovine serum albumin (BSA) was prepared using cupric ion as the bridge between the template BSA and the functional monomer 4‐vinylpyridine. N‐Isopropylacrylamide (NIPA) was used as an assistant monomer to provide the stimuli‐responsibility of the polymer. The adsorption conditions of BSA on the BSA‐Cu(II)‐imprinted hydrogel were optimized considering the influences of pH, temperature, and salt concentration. The proteins bound on the imprinted hydrogel can be easily recovered under mild conditions by using 10 mmol/L ethylene diamine tetraacetic acid (EDTA) (pH 7.0) containing 150 mmol/L NaCl as the eluting solution. The imprinting effect and adsorption capacity of the polymer were found to be significantly improved compared to the hydrogel prepared in the absence of cupric ion. The results demonstrated the advantages of using a template‐metal ion‐monomer coordination system to strengthen the interaction between the protein and monomer. The effects of different metals ions including Zn(II), Ni(II), Co(II), Cd(II), and Al(III) on the recognition ability of the BSA‐Cu(II)‐imprinted hydrogel were also investigated. The polymer showed high selectivity toward both the template protein and the cupric ion.
📜 SIMILAR VOLUMES
## Abstract We introduce a new type of molecular imprinted polymer (MIP) with immobilized assistant recognition polymer chains (ARPCs) to create effective recognition sites. In this work, cloned pig cyclophilin 18 (pCyP18) and BSA were used as templates, respectively. The template protein was selec
## Abstract Permeability‐surface area products (PAs) of the blood‐nerve barrier (BNB) and blood‐brain barrier (BBB) to ^125^I‐labeled native bovine serum albumin (nBSA, pI ∼︁4), and to 2 cationized albumins (cBSA) of differing pI (pI ∼︁ 8 and 11), were quantitatively determined in awake rats, using