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Inteins and affinity resin substitutes for protein purification and scale up
The development of self-cleaving fusion-tag technology has greatly simplified the purification of recombinant proteins at laboratory scale. The self-cleaving capability of these tags has recently been combined with additional purification tags to generate novel and convenient protein purification me...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2005
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1310522/ https://www.ncbi.nlm.nih.gov/pubmed/16283936 http://dx.doi.org/10.1186/1475-2859-4-32 |
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author | Banki, Mahmoud Reza Wood, David W |
author_facet | Banki, Mahmoud Reza Wood, David W |
author_sort | Banki, Mahmoud Reza |
collection | PubMed |
description | The development of self-cleaving fusion-tag technology has greatly simplified the purification of recombinant proteins at laboratory scale. The self-cleaving capability of these tags has recently been combined with additional purification tags to generate novel and convenient protein purification methods at a variety of scales. In this review, we describe some of these methods, and provide a rudimentary economic analysis of hypothetical large-scale applications. This work is expected to provide a rough outline for the evaluation of these methods for large-scale bioprocessing of a variety of products. |
format | Text |
id | pubmed-1310522 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-13105222005-12-10 Inteins and affinity resin substitutes for protein purification and scale up Banki, Mahmoud Reza Wood, David W Microb Cell Fact Review The development of self-cleaving fusion-tag technology has greatly simplified the purification of recombinant proteins at laboratory scale. The self-cleaving capability of these tags has recently been combined with additional purification tags to generate novel and convenient protein purification methods at a variety of scales. In this review, we describe some of these methods, and provide a rudimentary economic analysis of hypothetical large-scale applications. This work is expected to provide a rough outline for the evaluation of these methods for large-scale bioprocessing of a variety of products. BioMed Central 2005-11-11 /pmc/articles/PMC1310522/ /pubmed/16283936 http://dx.doi.org/10.1186/1475-2859-4-32 Text en Copyright © 2005 Banki and Wood; licensee BioMed Central Ltd. |
spellingShingle | Review Banki, Mahmoud Reza Wood, David W Inteins and affinity resin substitutes for protein purification and scale up |
title | Inteins and affinity resin substitutes for protein purification and scale up |
title_full | Inteins and affinity resin substitutes for protein purification and scale up |
title_fullStr | Inteins and affinity resin substitutes for protein purification and scale up |
title_full_unstemmed | Inteins and affinity resin substitutes for protein purification and scale up |
title_short | Inteins and affinity resin substitutes for protein purification and scale up |
title_sort | inteins and affinity resin substitutes for protein purification and scale up |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1310522/ https://www.ncbi.nlm.nih.gov/pubmed/16283936 http://dx.doi.org/10.1186/1475-2859-4-32 |
work_keys_str_mv | AT bankimahmoudreza inteinsandaffinityresinsubstitutesforproteinpurificationandscaleup AT wooddavidw inteinsandaffinityresinsubstitutesforproteinpurificationandscaleup |