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Amino Acid Sequences of Trypsin-Chymotrypsin Inhibitors (A-I, A-II, B-I, and B-II) from Peanut (Arachis hypogaea)1: A Discussion on the Molecular Evolution of Legume Bowman-Birk Type Inhibitors
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1983
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Trypsin-chymotrypsin InhibitorsGlycobiologyA Phylogenetic TreeArachis HypogaeaAmino Acid SequencesEnzymatic ModificationBiosynthesisProteomicsInhibitory ActivityAmino Acid DifferencesBiochemistryPharmacologyNatural SciencesPeptoidPeptide SynthesisPeanut Protease InhibitorsProtein EngineeringMedicineDrug Discovery
The amino acid sequences of four peanut protease inhibitors (A-I, A-II, B-I, and B-II) were determined by conventional methods and by comparison of peptide maps of their tryptic digests with that of B-III on HPLC. A-I, A-II, B-I, and B-III had the same amino acid sequence except for differences in their N-terminal regions. This suggests that the four inhibitors would be derived from an original inhibitor with a longer N-terminal amino acid sequence by proteolysis of its N-terminal region. But B-II possessed an extremely different amino acid sequence from those of the other peanut inhibitors and was thought to be biosynthesized from a gene different from that of the other inhibitors. A phylogenetic tree of legume double-headed inhibitors was constructed on the basis of the matrix of amino acid differences among their sequences. The double-headed inhibitors whose sequences have been determined were classified into four groups.