Conversion of Brain-Specific Complex Type Sugar Chains by N-Acetyl-.BETA.-D-Hexosaminidase B.
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概要
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The N-linked sugar chains, GlcNAcβ1-2Manα1-6(GlcNAcβ1-4)(Manα1-3)Manβ1-4GlcNAcβ1-4(Fucα1-6)GlcNAc (BA-1) and GlcNAcβ1-2Manα1-6(GlcNAcβ1-4)(GlcNAcβ1-2Manα1-3)Manβ1-4GlcNAcβ1-4(Fucα1-6)GlcNAc (BA-2), were recently found to be linked to membrane proteins of mouse brain in a development-dependent manner [S. Nakakita, S. Natsuka, K. Ikenaka, and S. Hase, J. Biochem. 123, 1164-1168 (1998)]. The GlcNAc residue linked to the Manα1-3 branch of BA-2 is lacking in BA-1 and the removal of this GlcNAc residue is not part of the usual biosynthetic pathway for N-linked sugar chains, suggesting the existence of an N-acetyl-β-D-hexosaminidase. Using pyridyl-aminated BA-2 (BA-2-PA) as a substrate the activity of this enzyme was found in all four subcellular fractions obtained. The activity was much greater in the cerebrum than in the cerebellum. To further identify the N-acetyl-β-D-hexosaminidase, BA-1 and BA-2 in brain tissues of Hex gene-disrupted mutant mice were detected and quantified. PA-sugar chains were liberated from the cerebrum and cerebellum of the mutant mice by hydrazinolysis-N-acetylation followed by pyridylamination. PA-sugar chains were separated by anion-exchange HPLC, size-fractionation, and reversed-phase HPLC. Each peak was quantified by measuring the peaks at the elution positions of authentic BA-1-PA and BA-2-PA. BA-2-PA was detected in all the PA-sugar chain fractions prepared from Hexa, Hexb, and both Hexa and Hexb (double knockout) gene-disrupted mice, but BA-1 was not found in the fractions from Hexb gene-disrupted and double knockout mice. These results indicate that N-acetyl-β-D-hexosaminidase B encoded by the Hexb gene hydrolyzed BA-2 to BA-1.
- 社団法人 日本生化学会の論文
著者
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IKENAKA Kazuhiro
National Institute for Physiological Sciences, Okazaki National Research Institutes
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Omichi Kaoru
Department Of Applied Chemistry Waseda University
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Yamanaka Shoji
Department Of Applied Chemistry Faculty Of Engineering Hiroshima University
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Ikenaka Kazuhiro
National Institute For Physiological Sciences
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Okamoto Yoshihisa
Department Of Bioregulation Nippon Medical School
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Hase Sumihiro
Department Of Chemistry Graduate School Of Science Osaka University
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