Cloning and sequence analysis of porcine myoglobin cDNA |
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Authors: | E Akaboshi |
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Affiliation: | Institute for Molecular and Cellular Biology, Osaka University, 1-3, Yamadaoka, Suita, 565 Japan Tel. (06)877-5111 |
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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. |
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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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