Glycosyltransferases in human respiratory tissue

摘要: Abstract Homogenates of human tracheobronchial tissue catalyzed the transfer sialic acid, galactose, fucose and N -acetylgalactosamine to glycoproteins sequentially treated with appropriate glycosidases. The optimal assay conditions kinetic properties these enzymes were determined using normal tissue. Since an abnormality in biosynthesis has been suspected pathogenesis chronic obstructive lung diseases, levels homogenates respiratory obtained at necropsy from subjects hypersecretion mucus. histological examination diseased ( n = 20) revealed hypertrophy mucous glands hyperplasia goblet cells. enzymatic assays demonstrated that, group, there was a twofold increase level activity both sialyltransferase (NAN GalNAc) galactosyltransferase (Gal GlcNAc), threefold -acetylgalactosaminyltransferase (GalNac protein) GalNAc), fourfold fucosyltransferase (Fuc GlcNAc) as compared 11). It appears that hypersecretory states humans may be associated synthesis either abnormal or proportions usual glycoproteins.