Abstract
Ten years ago, the purification of mammalian protein phosphatase 1 (PP1) was done routinely in only a handful of laboratories around the world. It typically involved the sacrifice of five rabbits and a cumbersome procedure that lasted 5 or 6 d, not to mention the requirement for heavy equipment, such as large-capacity centrifuges and tissue blenders. If all went well, you were rewarded with 1 or 2 mg of a close to homogeneously pure PP1 preparation. As in so many other instances, the classical purification of PP1 from its natural source has been supplanted by the recombinant DNA approach. This usually involves several steps, i.e., cloning of the gene or cDNA, subcloning the cDNA into a suitable vector, expressing the cDNA in a suitable host, and finally, purifying the recombinant protein.
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© 1998 Humana Press Inc.
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Dohadwala, M., Berndt, N. (1998). Expression of Functional Protein Phosphatase 1 Catalytic Subunit in E. coli . In: Ludlow, J.W. (eds) Protein Phosphatase Protocols. Methods in Molecular Biology™, vol 93. Humana Press. https://doi.org/10.1385/0-89603-468-2:191
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DOI: https://doi.org/10.1385/0-89603-468-2:191
Publisher Name: Humana Press
Print ISBN: 978-0-89603-468-6
Online ISBN: 978-1-59259-267-8
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