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.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Cloning, Molecular
  • Female
  • Gene Library
  • Humans
  • Liver / enzymology
  • Mice
  • Molecular Sequence Data
  • Open Reading Frames
  • Organ Specificity
  • Polymerase Chain Reaction
  • Pregnancy
  • Rats
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Sialyltransferases / biosynthesis*
  • Sialyltransferases / chemistry*
  • Sialyltransferases / metabolism
  • Swine
  • Transfection

Substances

  • Recombinant Proteins
  • Sialyltransferases
  • beta-galactoside alpha-2,3-sialyltransferase

Associated data

  • GENBANK/U63090