Wounding induces a series of closely related trypsin/chymotrypsin inhibitory peptides in leaves of tobacco

Phytochemistry. 1994 Nov;37(4):921-6. doi: 10.1016/s0031-9422(00)89505-9.


Wounding of tobacco (Nicotiana tabacum) leaves induced the expression of acid-stable trypsin/chymotrypsin inhibitory activity. Analysis by gel filtration determined that the inhibitory activity was contained within a fraction with a native M(r) of ca 5-7 x 10(3). Using ion-exchange column chromatography, this was resolved further into two major fractions, each of which inhibited both trypsin and chymotrypsin. Reverse-phase HPLC identified a total of six peptides from both fractions and each was purified to homogeneity. Four of these peptides inhibited both trypsin and chymotrypsin, a fifth inhibited trypsin only, while the sixth inhibited chymotrypsin almost exclusively. Sequencing of the N-terminal revealed that each peptide had an identical amino acid sequence and that these proteins are similar to a series of trypsin/chymotrypsin inhibitory peptides that are expressed predominantly in the stigmas of Nicotiana alata flowers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Chromatography, Ion Exchange
  • Chymotrypsin / antagonists & inhibitors*
  • Molecular Sequence Data
  • Nicotiana / physiology*
  • Plant Proteins / biosynthesis*
  • Plant Proteins / isolation & purification
  • Plants, Toxic*
  • Trypsin Inhibitors / biosynthesis*
  • Trypsin Inhibitors / isolation & purification


  • Plant Proteins
  • Trypsin Inhibitors
  • Chymotrypsin