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Proteinase Inhibitor Gene Families: Tissue Specificity and Regulation

  • Clarence A. Ryan
Part of the Plant Gene Research book series (GENE)

Abstract

Proteinase inhibtors are a multifamily group of proteins that are ubiquitous in nature (Laskowski, Jr. and Kato, 1984). Inhibitor proteins have been isolated that specifically inhibit each of the four known mechanistic classes of proteolytic enzymes, i. e. serine, thiol, aspartyl and metalloproteinases. Overall, the serine proteinase inhibitors comprise over ten unrelated protein families (Laskowski, Jr., 1986) that are found within the animal and plant kingdoms (Table 1). The functional role of these inhibitor proteins appears to be either to protect tissues or fluids from proteolysis by foreign proteases or to regulate the levels of proteases that are metabolically active in the tissues or fluids that they are associated with. The majority of proteinase inhibitor proteins that have been purified from plants have been inhibitors of serine endopeptidases such as the animal digestive enzymes trypsin, chymotrypsin and elastase or the bacterial proteinase subtilisin. In plants, the inhibitor proteins usually account for from 1 – 15 % or more of the proteins of various storage organs such as seeds and tubers (Ryan, 1974) and in some plant species, in leaves, in fruit, or in both (see below).

Keywords

Lectin Gene Kunitz Trypsin Inhibitor Proteinase Inhibitor Gene Wild Tomato Species Soybean Kunitz Trypsin Inhibitor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag/Wien 1988

Authors and Affiliations

  • Clarence A. Ryan
    • 1
  1. 1.Institute of Biological ChemistryWashington State UniversityPullmanUSA

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