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Cloning and sequence analysis of porcine myoglobin cDNA
Authors:E Akaboshi
Affiliation:Institute for Molecular and Cellular Biology, Osaka University, 1-3, Yamadaoka, Suita, 565 Japan Tel. (06)877-5111
Abstract:Porcine myoglobin cDNA clones have been isolated from a cDNA library prepared from enriched heart-myoglobin mRNA. Sequence analysis revealed 59 nucleotides (nt) in the 5'-untranslated, 462 nt in the amino acid (aa)-coding, and 590 nt in the 3'-untranslated regions. The myoglobin cDNA showed a high G + C content (60%). When the nt sequence of the porcine myoglobin cDNA is compared with those of seal and human myoglobin cDNAs deduced from the corresponding genomic myoglobin genes [Blanchetot et al., Nature 301 (1983) 732-734; Weller et al., EMBO J. 3 (1984) 439-446; Akaboshi, Gene 33 (1985) 241-249], a high degree of homology is observed in the 5'-untranslated region and in parts of the 3'-untranslated region, as well as in the coding region.
Keywords:Hybrid-arrested translation  nucleotide sequencing  human and seal myoglobin genes  introns  aa  amino acid(s)  cDNA  DNA complementary to mRNA  ds  double-stranded  nt  nucleotide(s)  ORF  open reading frame  p  plasmid  PA  polyacrylamide  SDS  sodium dodecyl sulfate  ss  single-stranded
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