Publication: Molecular cloning and domain structure of chicken pyruvate carboxylase
Issued Date
2002-01-01
Resource Type
ISSN
0006291X
Other identifier(s)
2-s2.0-0036069849
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Mahidol University
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SCOPUS
Bibliographic Citation
Biochemical and Biophysical Research Communications. Vol.295, No.2 (2002), 387-393
Suggested Citation
Sarawut Jitrapakdee, Mark G. Nezic, A. Ian Cassady, Yeesim Khew-Goodall, John C. Wallace Molecular cloning and domain structure of chicken pyruvate carboxylase. Biochemical and Biophysical Research Communications. Vol.295, No.2 (2002), 387-393. doi:10.1016/S0006-291X(02)00651-4 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/20103
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Title
Molecular cloning and domain structure of chicken pyruvate carboxylase
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 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.