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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/20103
Title: Molecular cloning and domain structure of chicken pyruvate carboxylase
Authors: Sarawut Jitrapakdee
Mark G. Nezic
A. Ian Cassady
Yeesim Khew-Goodall
John C. Wallace
University of Adelaide
Mahidol University
University of Queensland
Institute of Medical and Veterinary Science Australia
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jan-2002
Citation: Biochemical and Biophysical Research Communications. Vol.295, No.2 (2002), 387-393
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0036069849&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/20103
ISSN: 0006291X
Appears in Collections:Scopus 2001-2005

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