Mucin biosynthesis. Characterization of UDP-galactose: alpha-N-acetylgalactosaminide beta 3 galactosyltransferase from human tracheal epithelium.
作者： P W Cheng , S J Bona
DOI: 10.1016/S0021-9258(20)65131-6
关键词:
摘要: We have characterized the UDP-galactose: alpha-N-acetylgalactosaminide beta 3 galactosyltransferase in human tracheal epithelium using asialo ovine submaxillary mucin as acceptor. Maximal enzyme activity was obtained at pH 6.0-7.5 and 20-25 mM MnCl2 2% Triton X-100. Cd2+ could substitute for Mn2+ divalent ion cofactor. Spermine, spermidine, putrecine, cadaverine, poly-L-lysine stimulated low (2.5 mM) concentration. The apparent Michaelis constants N-acetylgalactosamine, mucin, UDP-galactose were 15.5, 1.14, 1.36 mM, respectively. not affected by alpha-lactalbumin. alpha-N-acetygalactosaminide shown to be different from N-acetylglucosamine acceptor competition studies. product of identified Gal 1 leads 3GalNAc alpha Ser (Thr) (a) isolation [14C]Gal-GalNAc-H2 after alkaline borohydride treatment 14C-labeled product, (b) establishment beta-configuration newly synthesized glycosidic bond its complete cleavage bovine testicular beta-galactosidase, (c) assignment linkage identification threosaminitol oxidation disaccharide with periodic acid followed reduction sodium borohydride, hydrolysis 4 N HCl, analysis on an amino analyzer. confirmed resistance jack bean beta-galactosidase presence a m/e 307 fragment absence 276 gas-liquid chromatography-mass spectrometry analysis. When beta-galactosidase-treated tracheobronchial used acceptor, 3.3% found [14C]Gal-GalNAc-H2. remainder [14C]Gal longer oligosaccharides formed beta-galactosyltransferase. This is slightly inhibited alpha-lactalbumin spermine.
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