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The search for the proteinase inhibitor-inducing factor, PIIF

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10 Years Plant Molecular Biology

Abstract

Research into the structure and function of proteinase Inhibitors I and II proteins in organs and tissues of several solanaceous plants began with the discovery and crystallization of Inhibitor I from Russet Burbank potato tubers in 1962 [1]. This was later followed by the isolation and characterization of Inhibitor II from potato tubers [2]. Inhibitor I and II are serine proteinase inhibitors that have evolved as members of two nonhomologous gene families. Inhibitor I proteins have a molecular mass of about 8000 kDa, whereas Inhibitor II proteins have a M r of about 12 000 kDa. Inhibitor I is a potent inhibitor of chymotrypsin, while Inhibitor II is a ‘double-headed’ inhibitor, having evolved by gene duplicated-elongation events from a smaller ancestral gene, and it possesses two reactive sites that are specific for trypsin and chymotrypsin respectively.

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  1. Institute for Biological Chemistry, Washington State University, Pullman, WA, 99164-6340, USA

    Clarence A. Ryan

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Robbert A. Schilperoort Leon Dure

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Ryan, C.A. (1992). The search for the proteinase inhibitor-inducing factor, PIIF. In: Schilperoort, R.A., Dure, L. (eds) 10 Years Plant Molecular Biology. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2656-4_8

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  • DOI: https://doi.org/10.1007/978-94-011-2656-4_8

  • Publisher Name: Springer, Dordrecht

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