FAST AND CHEAP PROTEIN PURIFICATION: Economical alternatives to conventional chromatography-based recombinant protein purification

 
9783639154436: FAST AND CHEAP PROTEIN PURIFICATION: Economical alternatives to conventional chromatography-based recombinant protein purification

Two naturally produced in vivo affinity resin substitutes have been combined with a self-cleaving tag to develop two novel affinity-based purification technologies. The first resin alternative is polyhydroxybutyrate (PHB) granules and the second is elastin-like polypeptides (ELP). An engineered tripartite protein fusion is expressed in E. coli and purified through simple centrifugation. The intein self-cleaving tag then releases the target protein with a mild pH shift. The two systems have been successfully used at laboratory scale to purify more than a dozen proteins varying in size, complexity and activity, demonstrating the proof of principle, high purity and yield attainable. Hence, the cost associated with purification of recombinant proteins is reduced significantly to effectively that of just the culture medium. It is expected that this combination of improved economics and simplicity will constitute a significant breakthrough in both large-scale production of purified proteins and enzymes as well as high-throughput proteomics studies.

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About the Author:

Mahmoud Reza Banki holds a BS in chemical engineering and a BA in applied mathematics from University of California at Berkeley. This work is mostly the outcome of his PhD work at the chemical engineering department at Princeton University and was partially sponsered by a National Science Foundation fellowship.

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Book Description Book Condition: New. Publisher/Verlag: VDM Verlag Dr. Müller | Economical alternatives to conventional chromatography-based recombinant protein purification | Two naturally produced in vivo affinity resin substitutes have been combined with a self-cleaving tag to develop two novel affinity-based purification technologies. The first resin alternative is polyhydroxybutyrate (PHB) granules and the second is elastin-like polypeptides (ELP). An engineered tripartite protein fusion is expressed in E. coli and purified through simple centrifugation. The intein self-cleaving tag then releases the target protein with a mild pH shift. The two systems have been successfully used at laboratory scale to purify more than a dozen proteins varying in size, complexity and activity, demonstrating the proof of principle, high purity and yield attainable. Hence, the cost associated with purification of recombinant proteins is reduced significantly to effectively that of just the culture medium. It is expected that this combination of improved economics and simplicity will constitute a significant breakthrough in both large-scale production of purified proteins and enzymes as well as high-throughput proteomics studies. | Format: Paperback | Language/Sprache: english | 195 gr | 136 pp. Bookseller Inventory # K9783639154436

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Book Description VDM Verlag Jul 2009, 2009. Taschenbuch. Book Condition: Neu. Neuware - Two naturally produced in vivo affinity resin substitutes have been combined with a self-cleaving tag to develop two novel affinity-based purification technologies. The first resin alternative is polyhydroxybutyrate (PHB) granules and the second is elastin-like polypeptides (ELP). An engineered tripartite protein fusion is expressed in E. coli and purified through simple centrifugation. The intein self-cleaving tag then releases the target protein with a mild pH shift. The two systems have been successfully used at laboratory scale to purify more than a dozen proteins varying in size, complexity and activity, demonstrating the proof of principle, high purity and yield attainable. Hence, the cost associated with purification of recombinant proteins is reduced significantly to effectively that of just the culture medium. It is expected that this combination of improved economics and simplicity will constitute a significant breakthrough in both large-scale production of purified proteins and enzymes as well as high-throughput proteomics studies. 140 pp. Englisch. Bookseller Inventory # 9783639154436

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Book Description VDM Verlag Jul 2009, 2009. Taschenbuch. Book Condition: Neu. Neuware - Two naturally produced in vivo affinity resin substitutes have been combined with a self-cleaving tag to develop two novel affinity-based purification technologies. The first resin alternative is polyhydroxybutyrate (PHB) granules and the second is elastin-like polypeptides (ELP). An engineered tripartite protein fusion is expressed in E. coli and purified through simple centrifugation. The intein self-cleaving tag then releases the target protein with a mild pH shift. The two systems have been successfully used at laboratory scale to purify more than a dozen proteins varying in size, complexity and activity, demonstrating the proof of principle, high purity and yield attainable. Hence, the cost associated with purification of recombinant proteins is reduced significantly to effectively that of just the culture medium. It is expected that this combination of improved economics and simplicity will constitute a significant breakthrough in both large-scale production of purified proteins and enzymes as well as high-throughput proteomics studies. 140 pp. Englisch. Bookseller Inventory # 9783639154436

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