J. Biochem, 2003, Vol. 134, No. 2 287-296
© 2003 Japanese Biochemical Society
BIOCHEMISTRY |
Comparison of the Enzymatic Properties of Mouse ß-Galactoside 
2,6-Sialyltransferases, ST6Gal I and II
,11 Laboratory of Cellular Biochemistry, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198; and 2 Molecular Glycobiology, The Glycoscience Institute, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112-8610
The cDNA encoding a second type of mouse ß-galactoside 
2,6-sialyltransferase (ST6Gal II) was cloned and characterized. The sequence of mouse ST6Gal II encoded a protein of 524 amino acids and showed 77.1% amino acid sequence identity with human ST6Gal II. Recombinant ST6Gal II exhibited 2,6-sialyltransferase activity toward oligosaccharides that have the Galß1,4GlcNAc sequence at the nonreducing end of their carbohydrate groups, but it exhibited relatively low and no activity toward some glycoproteins and glycolipids, respectively. On the other hand, ST6Gal I, which has been known as the sole member of the ST6Gal-family for more than ten years, exhibited broad substrate specificity toward oligosaccharides, glycoproteins, and a glycolipid, paragloboside. The ST6Gal II gene was mainly expressed in brain and embryo, whereas the ST6Gal I gene was ubiquitously expressed, and its expression levels were higher than those of the ST6Gal II gene. The ST6Gal II gene is located on chromosome 17 and spans over 70 kb of mouse genomic DNA consisting of at least 6 exons. The ST6Gal II gene has a similar genomic structure to the ST6Gal I gene. In this paper, we have shown that ST6Gal II is a counterpart of ST6Gal I.
* Special postdoctoral researcher from RIKEN.
To whom correspondence should be addressed. Tel: +81-48-467-9370, Fax: +81-48-462-4670, E-mail: tsujimot{at}postman.riken.go.jp
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