Two polypeptides with antiproteolytic activities have been isolated from alfalfa leaves. Polypeptide I resembles the previously described plant protease inhibitors in both structural and functional features; it has a molecular weight of 15,000, a random coil secondary structure, and inhibits exogenous protease as well as alfalfa leaf protease. Polypeptide II is a novel type of plant inhibitor with a molecular weight of 6300 and a highly organized structure with a high (40-50%) ?-helix content. It only inhibits endogenous protease with a molar stoichiometry polypeptide/enzyme protein of 1. © 1985.
Purification and characterization of two leaf polypeptide inhibitors of leaf protease from alfalfa (Medicago sativa)
Gonnelli;Ma;Cioni;Pa;Romagnoli;Gabellieri;
1985
Abstract
Two polypeptides with antiproteolytic activities have been isolated from alfalfa leaves. Polypeptide I resembles the previously described plant protease inhibitors in both structural and functional features; it has a molecular weight of 15,000, a random coil secondary structure, and inhibits exogenous protease as well as alfalfa leaf protease. Polypeptide II is a novel type of plant inhibitor with a molecular weight of 6300 and a highly organized structure with a high (40-50%) ?-helix content. It only inhibits endogenous protease with a molar stoichiometry polypeptide/enzyme protein of 1. © 1985.File in questo prodotto:
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