IDENTIFICATION OF LECTINS IN THE KINETIDS OF TETRAHYMENA PYRIFORMIS

Abstract

Previously we described lectin-like molecules in the ciliate Tetrahymena pyriformis; by application of synthetic neoglycoconjugates it is now shown that T. pyriformis contains considerable amounts of both a beta-D-glucose- and a lactose-specific lectin. No evidence for the presence of alpha-D-mannose-, alpha-D-galactose- or of alpha-L-fucose-specific lectins could be obtained. The two lectins, identified in T. pyriformis, are associated with the kinetids. During cell division the lectins disappear or become masked in the fission furrow. Therefore, we assume that these lectins are involved in the organization of the distribution pattern of the kinetids during cell division perhaps due to lectin-glycoprotein interactions.

Characterisation of carbohydrate-binding sites in developmental stages of Myxobolus cerebralis

“…Binding sites in fish skin were detected both by Danguy and Genten (1989) and Danguy et al (1991). In protozoans, glycohistochemistry has only been used on Tetrahymina piriformis, an ectocommensal of aquatic organisms (Kova`cs et al 1997): it was shown that this ciliate contains considerable amount of lectin activity specific for b-d-glucose-and lactose-motifs.…”