Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Molecular cloning and domain structure of chicken pyruvate carboxylase|
|Citation:||Biochemical and Biophysical Research Communications, 2002; 295(2):387-393|
|Publisher:||Academic Press Inc|
|Sarawut Jitrapakdee, Mark G. Nezic, A. Ian Cassady, Yeesim Khew-Goodall and John C. Wallace|
|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 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.|
|Appears in Collections:||Molecular and Biomedical Science publications|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.