Primary structure of Vicia angustifolia proteinase inhibitor.
The complete amino acid sequence (72 amino acid residues) of a double-headed proteinase inhibitor from seeds of Vicia angustifolia L. var. segetalis Koch has been determined and compared with those of other double-headed inhibitors of known structure. Sequencing was performed by conventional methods with the aid of the fragments produced by reduction and S-carboxymethylation of the enzymatically modified inhibitors, and also using tryptic and chymotryptic peptides. The positions of the 14 half-cystine residues agreed among all the reported primary structures of the legume double-headed inhibitors. However, V. angustifolia inhibitor possessed extensive amino acid differences compared to the others. The phylogenetic relationship among these inhibitors was established using the unweighted pair-group method and revealed that the V. angustifolia inhibitor and the peanut inhibitor B-III had diverged at a relatively earlier stage compared to the other inhibitors.
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin; D007887:Fabaceae / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D010946:Plants, Medicinal; D011480:Protease Inhibitors / Q000302:isolation & purification*; D014357:Trypsin
D010446:Peptide Fragments; D011480:Protease Inhibitors; D002918:Chymotrypsin; D014357:Trypsin