Isolation and characterization of a partial cDNA for a human sialyltransferase

Peter Lance, Karen M. Lau, Joseph T.Y. Lau

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


A probe generated from the coding sequence of the rat hepatic β-galactoside α2,6-sialyltransferase was used to screen a human cDNA library constructed of human submaxillary gland mRNA lambda gt-11. We report the isolation and characterization of a human cDNA, HSM-ST1, that is putatively the human homolog of the β-galactoside α2,6-sialyltransferase. The largest human clone contains a 1.3 kb cDNA insert and is predicted to encompass 75% of the coding sequence as well as a small portion of the 3′ untranslated region. Comparative analysis of this insert with the rat hepatic α2,6-sialyltransferase sequence indicates 79% nucleotide similarity between the two sequences in the predicted coding region. On the amino acid level, the degree of conservation is 86%. Substantial sequence similarity is observed in the 3′-untranslated region between the rat and human sequences as well. S1 nuclease analysis was performed to demonstrate the expression of HSM-ST1 transcripts in the human hepatoma cell line, HepG2, and in the human colonic adenocarcinoma cell lines, LS174T.

Original languageEnglish (US)
Pages (from-to)225-232
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Oct 16 1989

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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