GLYCOPROTEIN CHARACTERIZATION OF THE GELATINOUS MATRIX IN THE ROOT-KNOT NEMATODE MELOIDOGYNE-JAVANICA

Proteinaceous components of freshly formed gelatinous matrix (GM) of t he root-knot nematode Meloidogyne javanica were analyzed. Under reduci ng conditions, the prominent protein fragments had molecular weights o f 26 to 66 kDa and 150 to > 200 kDa, and most were glycosylated. Most of the fragments were digested by proteinase K, and fewer by trypsin. The lectins soybean agglutinin (SBA), Ulex europaeus agglutinin, and w heat germ agglutinin labeled the higher molecular weight bands (i.e., > 200 kDa). SBA labeled additional protein fractions between 26 and 66 kDa. Although Bandeiraea simplicifolia lectin and Concanavalin A did not label bands on the Western blot, they did label the GM in the dot blot technique. Analysis of amino acids and amino sugars in the GM rev ealed an unusually high amount of ammonia and galactosamine moieties.