원문정보
초록
영어
Sialyltransferases catalyze the transfer of sialic acid residues to nonreducing terminal position of glycoconjugates, using CMP-Neu5Ac as the donor. In the present study, a putative sialyltransferase Csav-ST3GalI/II gene identified from the marine invertebrate Ciona savignyi was expressed in yeast and CHO-K1 cell and functionally characterized using the Human-ST3Gal I sialyltransferase as a control. The expressions of recombinant sialyltransferases in transformed yeast and transfected CHO-K1 cells were confirmed at transcriptional and translational levels by using RT-PCR, SDS-PAGE, and western blot analysis. Furthermore, these enzymes were shown to be targeted in Golgi membranes in yeast and CHO-K1 cells by fluorescence image analysis of localization of green fluorescence protein-tagged sialyltransferases. Currently, we are investigating the biochemical properties of the recombinant Csav- ST3Gal I/II and the impacts of its expression in CHO-K1 cells on the glycan structures of glycoproteins by using various analytical techniques. Supported by a grant of the Marine and Extreme Genome Research Center Program funded by the Korean Ministry of Land, Transport, and Maritime Affairs.