Biological Chemistry Hoppe-Seyler · 1987 · 31 citations · 5 references
Life SciencesBotanyPlant SciencesEnzymologyPlant BiochemistryPlant Molecular BiologyEnzyme InhibitionPlant EnzymesProtein Sequence AnalysisProtein StructureSeed BiochemistryHomologyPlant ProteasesPlant Protein IdentificationPlant Protein SourcesSeed Protein Amino Acid CompositionSeed-associated EnzymesSquash And StretchStructural Homology
The amino-acid sequences of two trypsin inhibitors isolated from red bryony (Bryonia dioica) and watermelon (Citrullus vulgaris) seeds are reported. Both species represent different genera of the Cucurbitaceae family, which have not been previously investigated as a source of proteinase inhibitors. The sequences are unique but are very similar to those of other proteinase inhibitors which have been isolated from squash seeds. Based on structural homology we assume that the Arg5-Ile6 peptide bond represents the reactive site bond of both inhibitors.
5
Friedrich Lottspeich · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · 1980 · 214 citations
Maciej Wieczorek, Jacek Otlewski, James Cook et al. · Biochemical and Biophysical Research Communications · 1985 · 118 citations
Life Sciences, Biochemistry, Botany +17