Precise recognition of "brain-type" .BETA.1-4galactosyltransferase.

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  • 脳特異的糖鎖とその生合成に関わる“脳型”ガラクトース転移酵素
  • ノウ トクイテキ トウサ ト ソノ セイゴウセイ ニ カカワル ノウガタ ガラクトース テンイ コウソ

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We have reported two brain-specific agalactobiantennary N-linked sugar chains with the bisecting GlcNAc and α1-6Fuc residues, (GlcNAcβ1-2)0 or 1Manα1-3(GlcNAcβ1-2Manα1-6)(GlcNAcβ1-4)Manβ1-4GlcNAcβ1-4(Fucα1-6)GlcNAc [Shimizu, H., Ochiai, K., Ikenaka, K., Mikoshiba, K., and Hase, S. (1993) J. Biochem. 114, 334-338]. Here, the reason of the absence of Gal on the sugar chains was analyzed through the detection of the other complex type sugar chains in brain. Sia-Gal or Gal on the GlcNAc residues of brain-specific agalactobiantennary N-linked sugar chains was not found. We therefore have investigated the substrate specificity of galactosyltransferase activities in brain by using as acceptor substrates pyridylamino derivatives of agalactobiantennary sugar chains with structural variations in the bisecting GlcNAc and α1-6Fuc residues. While the β1-4galactosyltransferases in liver and kidney could utilize all nine oligosaccharides as substrates, the β1-4galactosyltransferase(s) in brain could not utilize the agalactobiantennary sugar chain with both the bisecting GlcNAc and Fuc residues, but could utilize the other three acceptors. Similar results were obtained using glycopeptides with the agalactobiantennary sugar chains with or without the bisecting GlcNAc and α1-6Fuc residues as substrates. The β1-4galactosyltransferase activity of adult mouse brain thus appears to be responsible for producing the brain specific sugar chains and different from β1-4galactosyltransferase-I.

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