title: Distribution difference of lectin binding in salivary gland treated with sialidase and trypsin.
abstract: Histochemical evaluation of complex carbohydrates in the salivary glands from rodents following sialidase and trypsin treatment were reported by the use of lectins binding technique which specifically link to corresponding sugar residues in macromolecules. Lectin staining in salivary gland generally increased following 1 h sialidase treatment, particularly in guinea-pig specimens. Lectin staining followed by treatment of trypsin (30 min) showed in increase in staining which is characteristic of UEA-I lectin. In long duration treated sections, by either sialidase or trypsin, lectin staining usually decreased in salivary glands. In the present study, complex carbohydrates of salivary glands may be hydrolyzed and degraded by sialidase and trypsin treatments, and lectin binding affinity is then also enhanced due to exposed sugar residues in complex carbohydrates.
mesh_terms: D000818:Animals; D006224:Cricetinae; D005260:Female; D006168:Guinea Pigs; D008297:Male; D008647:Mesocricetus; D051379:Mice; D008815:Mice, Inbred Strains; D009439:Neuraminidase / Q000494:pharmacology*; D010306:Parotid Gland / Q000276:immunology; D051381:Rats; D011919:Rats, Inbred Strains; D011975:Receptors, Mitogen / Q000378:metabolism*; D012469:Salivary Glands / Q000166:cytology / Q000187:drug effects / Q000276:immunology*; D013361:Sublingual Gland / Q000276:immunology; D013363:Submandibular Gland / Q000276:immunology; D014357:Trypsin / Q000494:pharmacology*
chemical_list: D011975:Receptors, Mitogen; D009439:Neuraminidase; D014357:Trypsin