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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/513

Title: Optimization of immobilized metal ion affinity chromatography for single-step purification of recombinant ovine growth hormone expressed in escherichia coli
Authors: Gupta, V
Eshwari, A N S
Panda, A K
Agarwal, G P
Keywords: Escherichia coli
Immobilized metal ion affinity chromatography
Growth hormone
Proteins
Iminodiacetic acid
Issue Date: 2003
Citation: Journal of Chromatography A, 998(1-2), 93–101
Abstract: In the present investigation, Sepharose 6B gel with 1,4-butanediol diglycidyl ether as spacer arm, iminodiacetic acid as the 21 21 ligand and Cu , Ni as metal ions were used to prepare an immobilized metal ion affinity (IMA) gel. The binding capacities of recombinant ovine growth hormone (roGH) onto IMA gels were maximized in the packed bed column.Parameters influencing the purification efficiencies such as pH, ionic strength and flow-rate were optimized to achieve improved separation. The roGH was purified from inclusion bodies with an overall yield of 73.5% and purity of 94.3% using 21 21 a Cu –iminodiacetic acid (IDA) column. However, the Ni –IDA column was more successful in purifying the roGH from crude cell lysate in a single-step with a yield of 83% and purity of 92.5%.
URI: http://eprint.iitd.ac.in/dspace/handle/2074/513
Appears in Collections:Biochemical Engg. and Biotechnology

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