Isolation and characterization of human and canine gastric mucosal glycoproteins and their degradation by proteases and acid hydrolases.
High molecular weight glycoproteins were isolated and purified from canine antral and fundic mucosal tissue by means of non-degrading techniques. The results disclosed the advantage of urea extraction technique over the culture method in isolating the native glycoproteins. The glycoproteins were susceptible to degradation by protease, thus yielding low molecular weight glycopeptides. Chemical analysis of these glycopeptides and their parent macromolecules revealed that the oligosaccharide residues are attached to threonine, serine and proline residues of the protein chains. Similarly, high molecular weight glycoproteins isolated from human gastric gel mucin showed the same characteristics of canine gastric glycoproteins. Canine fundic glycoprotein or glycopeptide released their prosthetic carbohydrate groups under the lytic effect of fundic acid hydrolases.
D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002478:Cells, Cultured; D004285:Dogs; D005643:Fucose / Q000378:metabolism; D005690:Galactose / Q000378:metabolism; D005752:Gastric Mucins / Q000032:analysis*; D005753:Gastric Mucosa / Q000032:analysis* / Q000187:drug effects; D006023:Glycoproteins / Q000032:analysis* / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000494:pharmacology; D011402:Pronase
D002241:Carbohydrates; D005752:Gastric Mucins; D006023:Glycoproteins; D005643:Fucose; D006867:Hydrolases; D011402:Pronase; D005690:Galactose