LECTIN FROM THE LICHEN PELTIGERA-MEMBRANACEA (ACH) NYL - CHARACTERIZATION AND FUNCTION

A specific lectin was isolated from the lichen Peltigera membranacea a nd purified to homogeneity by two chromatographic steps - carboxymethy l cellulose and hydroxyl appatite. This lectin (PMA) was found to be s pecifically inhibited by N-acetyl D-galactosamine. Fluorescamine-label led PMA was used for microscopic visualization of its reaction with th e homologous and some heterologous Nostoc cells. It was shown that the highly specific antibodies raised against PMA distinguished among sev eral closely related species of Peltigera. These antibodies showed no affinity to the germ tubes from spores of Peltigera praetextata or P. canina. Partial sequence analysis of the PMA revealed no homology to a ny other known lectin, including NLA, the lectin of the cyanolichen Ne phroma laevigatum.