Cloning and Sequencing of a Full-Length cDNA of Mouse N-Acetylglucosamine (β1–4)Galactosyltransferase1

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Abstract
A full-length cDNA clone for mouse N-acetylglucosamine (β 12–4)galactosyltransferase (β1–4GT) [EC 2.4.1.90] and several clones diverged from the β12–4GT cDNA were isolated from a mouse F9 cDNA library and then sequenced. The fβ1–4GT cDNA has an open reading frame consisting of 399 amino acids. The homology at the amino acid level is 80 and 91% as to the partial sequences of bovine and human milk β12–4GT respectively. The general enzyme structure of the β1–4GT seems to be similar to that of a rat β-galactoside (α2–6) sialyltransferase. Junctions of the common and divergent regions of cDNA have dinucleotides, AG, suggesting that the variety of cDNA clones is generated through alternative splicing.

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