Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/28172
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Type: Journal article
Title: Molecular cloning and domain structure of chicken pyruvate carboxylase
Author: Jitrapakdee, S.
Nezic, M.
Cassady, A.
Khew-Goodall, Y.
Wallace, J.
Citation: Biochemical and Biophysical Research Communications, 2002; 295(2):387-393
Publisher: Academic Press Inc
Issue Date: 2002
ISSN: 0006-291X
1090-2104
Statement of
Responsibility: 
Sarawut Jitrapakdee, Mark G. Nezic, A. Ian Cassady, Yeesim Khew-Goodall and 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.
Keywords: Pyruvate carboxylase; Domain structure; Partial proteolysis; Peptide sequence; Chicken liver mRNA
Description: Copyright © 2002 Elsevier Science (USA). All rights reserved.
RMID: 0020020619
DOI: 10.1016/S0006-291X(02)00651-4
Appears in Collections:Molecular and Biomedical Science publications

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