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Cloning of a human liver UDP‐glucose pyrophosphorylase cDNA by complementation of the bacterial galU mutation
Author(s) -
Peng Hwei-Ling,
Chang Hwan-You
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80213-e
Subject(s) - complementation , complementary dna , biochemistry , peptide sequence , microbiology and biotechnology , homology (biology) , molecular cloning , mutant , enzyme , amino acid , cloning (programming) , biology , gene , computer science , programming language
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.