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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Peng HL,Chang HY

doi

10.1016/0014-5793(93)80213-e

subject

Has Abstract

pub_date

1993-08-23 00:00:00

pages

153-8

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)80213-E

journal_volume

329

pub_type

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