1. Academic Validation
  2. Molecular cloning and expression of human Gal beta 1,3GalNAc alpha 2,3-sialytransferase (hST3Gal II)

Molecular cloning and expression of human Gal beta 1,3GalNAc alpha 2,3-sialytransferase (hST3Gal II)

  • Biochem Biophys Res Commun. 1996 Nov 12;228(2):324-7. doi: 10.1006/bbrc.1996.1660.
Y J Kim 1 K S Kim S H Kim C H Kim J H Ko I S Choe S Tsuji Y C Lee
Affiliations

Affiliation

  • 1 Division of Molecular Glycobiology, Korea Research Institute of Bioscience and Biotechnology, (KRIBB), Taejon, South Korea.
Abstract

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.

Figures