ISOLATION, IDENTIFICATION, AND QUANTIFICATION OF LECTIN PROTEIN CONTENTS IN CHAMERION ANGUSTIFOLIUM L. DRIED RAW MATERIAL AND THE STUDY OF ITS ACTIVITY USING RATUSERYTROAGGLUTINATION

Objective: To isolate, identify and quantify lectin protein contents in Chamerion angustifolium L. dried raw material species namely; leaves in the flowering stage, buds, and flowers and the study of its activity.Methods: Lectin activity has been determined using the biological method called ratuserytroagglutination. This method is based on the formation of aggregates of lectins and rat erythrocytes using the floor amount of lectins that agglutinate erythrocytes as a unit of measurement. Additionally, the protein contents of the extracts have been determined using the Bradford assay method.Results: lectins activity from Chamerion angustifolium L. in leaves in the flowering stage, buds, and flowers were 2.72±0.06, 0.24±0.008, and 0.56±0.014 units/mg protein, respectively. The greatest lectins activity was in the leaves in the flowering stage followed by flowers and then in buds. Protein contents in leaves in the flowering stage, buds, and flowers were 4.71±0.03, 6.77±0.02, and 5.76±0.14 mg/mL, respectively.Conclusion: All proteins obtained from the Chamerion angustifolium L. plant raw material were shown to possess rat erythrocytes agglutinating activity. The crude extract of leaves in the flowering stage exhibited the strongest hemagglutinating activity of about 2.72 units/mg proteins, whereas the buds showed the lowest activity of about 0.24 units/mg proteins. It should be highlighted herein, although many plant lectins mimic the behavior of plant storage proteins, these lectins should not be classified as storage proteins.Â