1981 Volume 78 Issue 4 Pages 812-816
Some characteristics of UDP-galactosyl transferase, which transfers Gal from UDP-Gal to (GlcNAc and GalNAC) n-protein core on the later step of biosynthesis of gastric glycoproteins, were studied in the scraped rat gastric mucosa After scraping of gastric mucosa of Wister rats, it was homogenized, and the homogenate was centrifuged at 500 xg for 10 min. The supernatant was used as enzyme solution and asialo-agalacto-fetuin was used as acceptor protein. In our method UDP-galactosyl transferase activity and protein were able to measure in 1mg wet weight of gastric mucosa. This enzyme activities (U./kg protein) were determined to be less than 10 (n=3) at forstomach, 946±125 (n=5) at fundic gland area, 835±94.9 (n=3) at pyloric gland area. The biopsy specimen could be stored at-70°C for 2 months without loss of UDP-galactosyl transferase activity.
Nippon Shokakibyo Gakkai Zasshi
Nippon Shokakibyo Gakkai Zasshi Kou
