Cleavage of oligosaccharides by rat kidney sialidase. Influence of substrate structure

The specificity of the sialidase activity present in rat kidney cortex (12 000 X g pellet) was studied with various tritiated oligosaccharidic substrates: (i) alpha NeuAc2----3 beta Gal1----4Glc-itol[3H], alpha NeuAc2----6 beta Gal1----4Glc-itol[3H]. and alpha NeuAc2----8 alpha NeuAc2----3 beta Gal1----4Glc-itol[3H] from bovine colostrum; (ii) alpha NeuAc2----6 beta Gal1----4 beta GlcNAc-itol[3H], alpha NeuAc2----3 beta Gal1----4 beta GlcNAcl----2 alpha Man1----3 beta Man1----4 GlcNAc-itol[3H] alpha NeuAc2----6 beta Gal1----4 beta GlcNAc1----2 alpha Man1----3(beta Gal 1----4GlcNAc1----2 alpha Man 1----6)beta Man1----4GlcNAc-itol[3H]et alpha NeuAc2----6 beta Gal1----4 beta GlcNAc1----2 alpha Man1----3(alpha NeuAc2----6 beta Gal1----4 beta GlcNAc1----2 alpha Man1----6)beta Man1 4GlNAc-itol[3H] isolated from the urine of a patient with mucolipidosis I. The enzyme cleaves alpha 2----3 and alpha 2----8 linkages at a greater rate than the alpha 2----6 bonds. Its activity decreases with the length of the oligosaccharidic chain. Substitution of a glucose moiety by Nacetylglucosamine results in diminished activity. The specificity of rat kidney sialidase differs from that reported for other mammalian of viral sialidases.