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Biochem Biophys Res Commun. 1996 Nov 12;228(2):324-7.

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

Author information

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.

PMID:
8920913
DOI:
10.1006/bbrc.1996.1660
[Indexed for MEDLINE]

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