The primary sequence of Erythrina corallodendron lectin was deduced from analysis of the peptides derived from the lectin by digestion with trypsin, chymotrypsin, Staphylococcus aureus V8 protease, elastase and lysylendopeptidase-C, and of fragments generated by cleavage of the lectin with dilute
Plant Kunitz-type protease inhibitors contain a conserved Asn residue in the N-terminal region. To investigate the role of Asn residue in protease inhibitory activities, Erythrina variegata trypsin inhibitor a (ETIa), E. variegata chymotrypsin inhibitor (ECI), and their mutants, ETIa-N12A and
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