Cloning and sequence analysis of porcine myoglobin cDNA
1985; Elsevier BV; Volume: 40; Issue: 1 Linguagem: Inglês
10.1016/0378-1119(85)90033-2
ISSN1879-0038
Autores Tópico(s)RNA and protein synthesis mechanisms
ResumoPorcine 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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