Trypsin inhibitory activity of bovine fetuin de-O-glycosylated by endo-alpha-N-acetylgalactosaminidase.
The effects of bovine fetuin O-glycans on its trypsin inhibitory activity were examined. De-sialylated (asialo-) and de-O-glycosylated fetuin were prepared from native fetuin using Arthrobacter neuraminidase and the mixture of it and Bacillus endo-alpha-N-acetylgalactosaminidase, respectively. De-sialylation and de-O-glycosylation from fetuin were confirmed with SDS-PAGE followed by western blotting using anti-human Thomsen-Friedenreich antigen (T antigen) antibody which recognizes O-linked galactosyl beta1,3 N-acetylgalactosamine (Gal beta1-->3GalNAc). Native fetuin completely inhibited the trypsin activity at about a 1:1 molar ratio. In contrast, the trypsin inhibitory activity of asialo- and de-O-glycosylated fetuin decreased about a half and one-third of that of native fetuin, respectively.
Ashida
H
H
Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Japan. BYD01621@nifty.ne.jp
Yamamoto
K
K
Kumagai
H
H
D000818:Animals; D002417:Cattle; D006031:Glycosylation; D006596:Hexosaminidases / Q000494:pharmacology*; D014361:Trypsin Inhibitors / Q000494:pharmacology*; D000509:alpha-Fetoproteins / Q000378:metabolism*; D048809:alpha-N-Acetylgalactosaminidase
D014361:Trypsin Inhibitors; D000509:alpha-Fetoproteins; D006596:Hexosaminidases; C482722:NAGA protein, human; D048809:alpha-N-Acetylgalactosaminidase