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Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by complementation of the bacterial galU mutation
Journal article   Open access   Peer reviewed

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

Hwei-Ling Peng and Hwan-You Chang
FEBS Letters, Vol.329(1-2), pp.153-158
23/08/1993

Abstract

E. coli galU Glycogen UDP-glucose pyrophosphorylase cDNA
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. © 1993.
url
https://doi.org/10.1016/0014-5793(93)80213-EView
Published (Version of record) Open

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