Yj. Kim et al., MOLECULAR-CLONING AND EXPRESSION OF HUMAN GAL-BETA-1,3GALNAC ALPHA-2,3-SIALYLTRANSFERASE (HST3GAL-II), Biochemical and biophysical research communications, 228(2), 1996, pp. 324-327
A cDNA of human Gal beta 1,3GalNAc alpha 7,3-sialytransferase (hST3Gal
II), which has been known to exhibit much more acceptor substrate pre
ference for glycolipid than for O-linked oligosaccharides of glycoprot
eins, was isolated from the human liver cDNA library by plaque hybridi
zation using the cDNA of mouse ST3Gal II (mST3Gal II) cloned previousl
y as a probe. Comparative analysis of this cDNA with mST3Gal II indica
tes 89 and 94% homologies in the nucleotide and amino acid levels. res
pectively, between the two sequences in the predicted ending region. N
orthern analysis indicated that the expression of hSTSGal II mRNA is t
issue-specific, it bring prominent in skeletal muscle and heart, while
that in lung and kidney is very low. This enzyme expressed in COS cel
ls showed a similiar activity with that of mSTSGal II. (C) 1996 Academ
ic Press, Inc.