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PLANT PHYSIOLOGY , Vol 102, Issue 2 639-644, Copyright © 1993 by American Society of Plant Biologists
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ENVIRONMENTAL AND STRESS PHYSIOLOGY |
Purification and Characterization from Tobacco (Nicotiana tabacum) Leaves of Six Small, Wound-Inducible, Proteinase Isoinhibitors of the Potato Inhibitor II Family
G. Pearce, S. Johnson and C. A. Ryan
Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340
Six small molecular mass, wound-inducible trypsin and chymotrypsin
inhibitor proteins from tobacco (Nicotiana tabacum) leaves were isolated to
homogeneity. The isoinhibitors, cumulatively called tobacco trypsin
inhibitor (TTI), have molecular masses of approximately 5500 to 5800 D,
calculated from gel filtration analysis and amino acid content. The amino
acid sequence of the entire 53 residues of one isoinhibitor, TTI-1, and the
sequence of 36 amino acid residues from the N terminus of a second
isoinhibitor, TTI-5, were determined. The two isoinhibitors differ only at
residue 11, which is threonine in TTI-1 and lysine in TTI-5. The
isoinhibitors are members of the potato inhibitor II family and show
considerable identity with the small molecular mass members of this family,
which include the eggplant inhibitor, two small molecular mass trypsin and
chymotrypsin inhibitors from potatoes, and an inhibitor from pistils of the
ornamental plant Nicotiana alata. Antibodies produced against the
isoinhibitors in rabbits were used in radial immunoassays to quantify both
the systemic wound inducibility of TTI in tobacco leaves and its
constitutive levels in flowers.
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