Molecular cloning and expression of human Gal beta 1,3GalNAc alpha 2,3-sialytransferase (hST3Gal II).
A cDNA of human Gal beta 1,3GalNAc alpha 2,3-sialytransferase (hST3Gal II) which has been known to exhibit much more acceptor substrate preference for glycolipid than for O-linked oligosaccharides of glycoproteins, was isolated from the human liver cDNA library by plaque hybridization using the cDNA of mouse ST3Gal II (mST3Gal II) cloned previously as a probe. Comparative analysis of this cDNA with mST3Gal II indicates 89 and 94% homologies in the nucleotide and amino acid levels, respectively, between the two sequences in the predicted coding region. Northern analysis indicated that the expression of hST3Gal II mRNA is tissue-specific, it being prominent in skeletal muscle and heart, while that in lung and kidney is very low. This enzyme expressed in COS cells showed a similar activity with that of mST3Gal II.
Kim
Y J
YJ
Division of Molecular Glycobiology, Korea Research Institute of Bioscience and Biotechnology, (KRIBB), Taejon, South Korea.
Kim
K S
KS
Kim
S H
SH
Kim
C H
CH
Ko
J H
JH
Choe
I S
IS
Tsuji
S
S
Lee
Y C
YC
D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D003001:Cloning, Molecular; D005260:Female; D015723:Gene Library; D006801:Humans; D008099:Liver / Q000201:enzymology; D051379:Mice; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D009928:Organ Specificity; D016133:Polymerase Chain Reaction; D011247:Pregnancy; D051381:Rats; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012799:Sialyltransferases / Q000096:biosynthesis* / Q000737:chemistry* / Q000378:metabolism; D013552:Swine; D014162:Transfection; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase
D011994:Recombinant Proteins; D012799:Sialyltransferases; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase