Abstract
An agglutinin from plasma of the locust Locusta migratoria was purified to apparent homogeneity by one step affinity chromatography. Two kinds of affinity columns were used which gave the same results concerning 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, which 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 lectins. The purified agglutinin is heat resistant. Agglutination of RRBC required divalent cations. Some sugars were inhibitors of agglutination by crude plasma or by migratorin. Agglutination was also inhibited in both crude plasma and migratorin by antibodies raised against purified migratorin. These data indicate that agglutination observed in locust hemolymph was due to the protein we have purified.
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