The Adsorption of Calmoduline via Nicotinamide Immobilized Poly(HEMA-GMA) Cryogels

Yıl 2017, Cilt: 4 Sayı: 1, 133 - 148, 09.01.2017

Kadir Erol

https://doi.org/10.18596/jotcsa.287321

Cited By: 18

Öz

The separation and purification methods for the isolation of an important biomolecule calmoduline protein is extremely important. Among these methods, the adsorption technique is extremely popular, and the cryogels as adsorbents with the macro porous structure and interconnected flow channels cryogel they have are preferred in this field. In this study, the adsorption of calmoduline via Ca(II) immobilized poly (2-hydroxyethyl methacrylate-glycidyl methacrylate), poly (HEMA-GMA), cryogels through changing interaction time, calmoduline initial concentration and temperature conditions. For the characterization of cryogels, the swelling test, Fourier Transform Infrared (FT-IR) Spectroscopy, Scanning Electron Microscopy (SEM), surface area (BET), elemental analysis and ICP-OES methods were performed. Nicotinamide molecule was used as Ca (II) chelating agent and the adsorption capacity of the cryogels was estimated as 1.812 mg calmoduline / g cryogel. The adsorption models of the adsorption reaction were examined by the Langmuir and Freundlich isotherm models and was determined to be more appropriate for Langmuir isotherm model.

Anahtar Kelimeler

Adsorption, calmoduline; cryogel; nicotinamide.

Kaynakça

• Sudhakar Babu, Y., C. Bugg, and W. Cook, Structure of calmodulin refined at 2.2 Å resolution. Journal of molecular biology, 1988. 204(1): p. 191-204.
• Zhang, M., T. Tanaka, and M. Ikura, Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Structural & Molecular Biology, 1995. 2(9): p. 758-767.
• Hitoshi Kuboniwa, N.T., et al., Solution structure of calcium-free calmodulin. Nature structural biology, 1995. 2(9).
• Yamniuk, A.P. and H.J. Vogel, Calmodulin’s flexibility allows for promiscuity in its interactions with target proteins and peptides. Molecular biotechnology, 2004. 27(1): p. 33-57.
• Webb, R.C., Smooth muscle contraction and relaxation. Advances in physiology education, 2003. 27(4): p. 201-206.
• Means, A.R., Calcium, calmodulin and cell cycle regulation. FEBS letters, 1994. 347(1): p. 1-4.
• Racioppi, L. and A.R. Means, Calcium/calmodulin-dependent protein kinase kinase 2: roles in signaling and pathophysiology. Journal of Biological Chemistry, 2012. 287(38): p. 31658-31665.
• Kulej, K., et al., Optimization of calmodulin-affinity chromatography for brain and organelles. EuPA Open Proteomics, 2015. 8: p. 55-67.
• O'Day, D.H., CaMBOT: profiling and characterizing calmodulin-binding proteins. Cellular signalling, 2003. 15(4): p. 347-354.
• Clapham, D.E., Calcium signaling. Cell, 2007. 131(6): p. 1047-1058.
• Ikura, M., M. Osawa, and J.B. Ames, The role of calcium‐binding proteins in the control of transcription: structure to function. Bioessays, 2002. 24(7): p. 625-636.
• West, A.E., et al., Calcium regulation of neuronal gene expression. Proceedings of the National Academy of Sciences, 2001. 98(20): p. 11024-11031.
• Porath, J., et al., Metal chelate affinity chromatography, a new approach to protein fractionation. Nature, 1975. 258: p. 598-599.
• Block, H., et al., Immobilized-metal affinity chromatography (IMAC): a review. Methods in enzymology, 2009. 463: p. 439-473.
• Cheung, R.C.F., J.H. Wong, and T.B. Ng, Immobilized metal ion affinity chromatography: a review on its applications. Applied microbiology and biotechnology, 2012. 96(6): p. 1411-1420.
• Westra, D.F., et al., Immobilised metal-ion affinity chromatography purification of histidine-tagged recombinant proteins: a wash step with a low concentration of EDTA. Journal of Chromatography B: Biomedical Sciences and Applications, 2001. 760(1): p. 129-136.
• Yip, T.-T. and T.W. Hutchens, Immobilized metal-ion affinity chromatography. Protein Purification Protocols, 2004: p. 179-190.
• Charlton, A. and M. Zachariou, Immobilized metal ion affinity chromatography of histidine-tagged fusion proteins. Affinity Chromatography: Methods and Protocols, 2008: p. 137-150.
• Kågedal, L., Immobilized metal ion affinity chromatography. Protein Purification, Principles, High Resolution Methods, and Applications, 2011: p. 183-201.
• Karakus, C., et al., Evaluation of immobilized metal affinity chromatography kits for the purification of histidine-tagged recombinant CagA protein. Journal of Chromatography B, 2016. 1021: p. 182-187.
• Kose, K., et al., Affinity purification lipase from wheat germ: comparison of hydrophobic and metal chelation effect. Artif Cells Nanomed Biotechnol, 2016(2169-141X (Electronic)): p. 1-10.
• Erol, K., et al., Polyethyleneimine assisted-two-step polymerization to develop surface imprinted cryogels for lysozyme purification. Colloids Surf B Biointerfaces, 2016. 146: p. 567-76.
• Kose, K., et al., PolyAdenine cryogels for fast and effective RNA purification. Colloids Surf B Biointerfaces, 2016. 146: p. 678-86.
• Kose, K. and L. Uzun, PolyGuanine methacrylate cryogels for ribonucleic acid purification. J Sep Sci, 2016. 39(10): p. 1998-2005.
• Langmuir, I., The adsorption of gases on plane surfaces of glass, mica and platinum. Journal of the American Chemical society, 1918. 40(9): p. 1361-1403.
• Freundlich, H.M.F., Uber die adsorption in losungen. Zeitschrift fur Physikalische Chemie, 1906. 57: p. 385-471.