PURIFICATION AND CHARACTERIZATION OF AN AGGLUTININ FROM THE HEMOLYMPHOF LOCUSTA-MIGRATORIA (ORTHOPTERA)

An agglutinin from plasma of the locust Locusta migratoria ia was puri fied to apparent homogeneity by one step affinity chromatography. Two kinds of affinity columns were used which gave the same results concer ning the degree of purification. We named this agglutinin 'migratorin' . Its subunit M(r) is 80 kDa with no disulfide bounds. Measurements of M(r) of the native protein by Ferguson plots gave M(r) c. 650 kDa, wh ich means that the agglutinin is probably a polymer of 8 subunits. Its pI is 5.8. These M(r) and pI are similar to those of several insect l ectins. The purified agglutinin is heat resistant. Agglutination of RR BC required divalent cations. Some sugars were inhibitors of agglutina tion by crude plasma or by migratorin. Agglutination was also inhibite d in both crude plasma and migratorin by antibodies raised against pur ified migratorin. These data indicate that agglutination observed in l ocust hemolymph was due to the protein we have purified.