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|Title:||Molecular cloning and domain structure of chicken pyruvate carboxylase|
Mark G. Nezic
A. Ian Cassady
John C. Wallace
University of Adelaide
University of Queensland
Institute of Medical and Veterinary Science Australia
|Keywords:||Biochemistry, Genetics and Molecular Biology|
|Citation:||Biochemical and Biophysical Research Communications. Vol.295, No.2 (2002), 387-393|
|Abstract:||Pyruvate carboxylase (PC) [EC 126.96.36.199] 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 Mrof 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. © 2002 Elsevier Science (USA). All rights reserved.|
|Appears in Collections:||Scopus 2001-2005|
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