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Secretion of Recombinant Human Insulin-Like Growth Factor I (IGF-I)

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Pichia Protocols

Part of the book series: Methods in Molecular Biology ((MIMB,volume 103))

Abstract

The development of efficient recombinant protein production processes can be a critical factor in whether or not a pharmaceutical therapeutic protein can enter human clinical trials and ultimately the marketplace. This is especially true for therapeutic proteins that need to be administered on a daily basis for prolonged periods or if dosage requirements are very high. The use of Pichia pastoris as a recombinant expression host strain can be an excellent choice for such situations. P. pastoris has the potential for high expression levels (1,2), efficient secretion, and proper protein folding (3–5), and is a robust fermentation organism capable of high cell density on inexpensive simple basal salts medium (6). The development of an insulin-like growth factor I (IGF-I) production process in which P. pastoris is used as the recombinant host strain is discussed in this chapter.

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Author information

Authors and Affiliations

  1. Cephalon, Inc., Westchester, PA, USA

    Russell A. Brierley

Authors
  1. Russell A. Brierley
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Editor information

Editors and Affiliations

  1. Chiron Technologies/Center for Gene Therapy, San Diego, CA, USA

    David R. Higgins

  2. Oregon Graduate Institute of Science and Technology, Portland, OR, USA

    James M. Cregg

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© 1998 Humana Press Inc., Totowa, NJ

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Brierley, R.A. (1998). Secretion of Recombinant Human Insulin-Like Growth Factor I (IGF-I). In: Higgins, D.R., Cregg, J.M. (eds) Pichia Protocols. Methods in Molecular Biology, vol 103. Humana, Totowa, NJ. https://doi.org/10.1385/0-89603-421-6:149

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  • DOI: https://doi.org/10.1385/0-89603-421-6:149

  • Publisher Name: Humana, Totowa, NJ

  • Print ISBN: 978-0-89603-421-1

  • Online ISBN: 978-1-59259-578-5

  • eBook Packages: Springer Protocols

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