Purification and characterization from tobacco (Nicotiana tabacum) leaves of six small, wound-inducible, proteinase isoinhibitors of the potato inhibitor II family.

@article{Pearce1993PurificationAC,
  title={Purification and characterization from tobacco (Nicotiana tabacum) leaves of six small, wound-inducible, proteinase isoinhibitors of the potato inhibitor II family.},
  author={Gregory Pearce and Steven Johnson and Clarence A. Ryan},
  journal={Plant physiology},
  year={1993},
  volume={102 2},
  pages={639-44}
}
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… CONTINUE READING

From This Paper

Figures, tables, results, connections, and topics extracted from this paper.
43 Extracted Citations
0 Extracted References
Similar Papers

Citing Papers

Publications influenced by this paper.
Showing 1-10 of 43 extracted citations

Similar Papers

Loading similar papers…