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Plant Physiology 97:15-18 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Two Kunitz-Type Proteinase Inhibitors from Potato Tubers

Terence A. Walsh and Wayne P. Twitchell1

Agricultural Biotechnology Laboratory, DowElanco, 1701 Building, Midland, Michigan 48674

Two proteinase inhibitors have been isolated from tubers of potato (Solanum tuberosum). Based on N-terminal amino acid sequence homologies, they are members of the Kunitz family of proteinase inhibitors. Potato Kunitz inhibitor-1 (molecular weight 19,500, isoelectric point 6.9) is a potent inhibitor of the animal pancreatic proteinase trypsin, and its amino terminus has significant homology to a recently characterized cathepsin D Kunitz inhibitor from potato tubers (Mares et al. [1989] FEBS Lett 251:94-98). Potato Kunitz inhibitor-2 (molecular weight 20,500, isoelectric point 8.6) is an inhibitor of the microbial proteinase subtilisin Carlsberg; its amino terminus is almost identical to an abundant 22 kilodalton protein from potato tubers (Suh et al. [1990] Plant Physiol 94:40-45) and has significant homology to other Kunitz-type subtilisin inhibitors from small grains. Both Kunitz inhibitors are abundant proteins of the cortex of potato tubers.

1 Present address: Department of Biology, Lilly Hall, Purdue University, West Lafayette, IN 47907.




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P. Lison, I. Rodrigo, and V. Conejero
A Novel Function for the Cathepsin D Inhibitor in Tomato
Plant Physiology, November 1, 2006; 142(3): 1329 - 1339.
[Abstract] [Full Text] [PDF]


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Copyright © 1991 by the American Society of Plant Biologists