Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by complementation of the bacterial galU mutation

Hwei-Ling Peng, Hwan You Chang*

*Corresponding author for this work

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

A human liver cDNA clone which encodes the UDP-glucose pyrophosphorylase was isolated by complementation of a bacterial galU mutant. The deduced amino acid sequence of the human enzyme comprised 508 amino acids with a calculated molecular mass of 56,950. The human enzyme significantly resembles those of potato tuber and slime mold with a homology of 46.6% and 43.2%, respectively, in amino acid sequence. No homology was found between the eukaryotic and the prokaryotic enzymes. Northern blotting analysis revealed that the gene was expressed at the highest level in skeletal muscle, followed by liver, heart and kidney.

Original languageEnglish
Pages (from-to)153-158
Number of pages6
JournalFEBS Letters
Volume329
Issue number1-2
DOIs
StatePublished - 23 Aug 1993

Keywords

  • E. coli galU
  • Glycogen
  • UDP-glucose pyrophosphorylase cDNA

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