Archives of Biochemistry and Biophysics 1985-Apr
Purification and characterization of two leaf polypeptide inhibitors of leaf protease from alfalfa (Medicago sativa).
רק משתמשים רשומים יכולים לתרגם מאמרים
התחבר הרשם
הקישור נשמר בלוח
מילות מפתח
תַקצִיר
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%) alpha-helix content. It only inhibits endogenous protease with a molar stoichiometry polypeptide/enzyme protein of 1.