Title |
Molecular cloning and domain structure of chicken pyruvate carboxylase
|
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Published in |
Biochemical & Biophysical Research Communications, July 2002
|
DOI | 10.1016/s0006-291x(02)00651-4 |
Pubmed ID | |
Authors |
Sarawut Jitrapakdee, Mark G Nezic, A Ian Cassady, Yeesim Khew-Goodall, John C Wallace |
Abstract |
Pyruvate carboxylase (PC) [EC 6.4.1.1] is a biotin-dependent carboxylase that catalyses the conversion of pyruvate to oxaloacetate. Here we have determined the complete nucleotide sequence encoding chicken PC (cPC) by screening a liver cDNA library, by RT-PCR of poly(A)(+) RNA, and by PCR of genomic DNA. The full-length transcript contains an open reading frame of 3537 nucleotides, including the stop codon, encoding a polypeptide of 1178 amino acids with M(r) of 127,262. The amino acid sequence of cPC shows approximately 77% identity to mammalian PC. Limited proteolysis of pure cPC with chymotrypsin yields a major stable 75 kDa C-terminal peptide, including the biotinyl domain and a minor, unstable 39 kDa N-terminal peptide. Northern analysis of poly(A)(+) RNA isolated from chicken liver has shown that cPC's mRNA is approximately 5 kb in length, including a very long 3'-untranslated region. |
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Demographic breakdown
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