| First Author | Kojima N | Year | 1995 |
| Journal | FEBS Lett | Volume | 360 |
| Issue | 1 | Pages | 1-4 |
| PubMed ID | 7875291 | Mgi Jnum | J:28219 |
| Mgi Id | MGI:75844 | Doi | 10.1016/0014-5793(95)00059-i |
| Citation | Kojima N, et al. (1995) Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase activity toward N-linked oligosaccharides. FEBS Lett 360(1):1-4 |
| abstractText | 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. |
