RRC ID 57671
Author Kojima N, Yoshida Y, Kurosawa N, Lee YC, Tsuji S.
Title Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase activity toward N-linked oligosaccharides.
Journal FEBS Lett
Abstract We have detected sialyltransferase activity of recombinant mouse STX, which was cloned from rat brain as a new member of the sialyltransferase family, but sialyltransferase activity of which had not been detected previously [Livingston and Paulson, J. Biol. Chem. (1993) 268, 11504-11507]. The activity of mouse STX was specific toward sialylated glycoproteins. N-Glycanase treatment and linkage-specific sialidase treatment of glycoproteins revealed that STX transfers sialic acids through alpha 2,8-linkages to only N-linked oligosaccharides of glycoproteins. However, polymerase activity for polysialic acid synthesis was not detected for this sialyltransferase. Since this alpha 2,8-sialyltransferase gene is highly restricted in fetal and newborn brain, it may be involved in the polysialylation of glycoproteins, especially of N-CAM.
Volume 360(1)
Pages 1-4
Published 1995-2-20
DOI 10.1016/0014-5793(95)00059-i
PII 0014-5793(95)00059-I
PMID 7875291
MeSH Animals Base Sequence Cloning, Molecular DNA, Complementary Gene Expression Regulation, Enzymologic* Mice Molecular Sequence Data Oligosaccharides / metabolism* Sialyltransferases / genetics Sialyltransferases / metabolism*
IF 3.057
Times Cited 104
DNA material mST8SiaII (RDB02078)