Sarawut JitrapakdeeMark G. NezicA. Ian CassadyYeesim Khew-GoodallJohn C. WallaceUniversity of AdelaideMahidol UniversityUniversity of QueenslandInstitute of Medical and Veterinary Science Australia2018-07-242018-07-242002-01-01Biochemical and Biophysical Research Communications. Vol.295, No.2 (2002), 387-3930006291X2-s2.0-0036069849https://repository.li.mahidol.ac.th/handle/20.500.14594/20103Pyruvate 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1016/S0006-291X(02)00651-4