dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:17:31Z
dc.date.accessioned2022-10-05T15:57:01Z
dc.date.available2014-05-20T15:17:31Z
dc.date.available2022-10-05T15:57:01Z
dc.date.created2014-05-20T15:17:31Z
dc.date.issued2007-01-01
dc.identifierGenetics and Molecular Biology. Sociedade Brasileira de Genética, v. 30, n. 4, p. 1089-1092, 2007.
dc.identifier1415-4757
dc.identifierhttp://hdl.handle.net/11449/30502
dc.identifier10.1590/S1415-47572007000600010
dc.identifierS1415-47572007000600010
dc.identifier2-s2.0-37649020453
dc.identifierS1415-47572007000600010.pdf
dc.identifier1926863917378909
dc.identifier8858800699425352
dc.identifier0000-0003-4600-0367
dc.identifier0000-0003-3534-974X
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3903385
dc.description.abstractAn alpha actin gene segment, isolated from Nile tilapia (Oreochromis niloticus), was characterized by nucleotide sequencing, predicted amino acid sequence and Southern blot hybridization. Genomic DNA amplification resulted in a 1063-bp fragment corresponding to a partial alpha-cardiac muscle actin gene containing exons 3 to 6. Southern blot analysis of the restriction-digested DNA revealed that the Nile tilapia genome contains multiple muscle actin isoforms. Although comparison of the nucleotide sequence, amino acid residues and exon-intron organization of the isolated actin gene with those of other vertebrates showed a high level of identity, diagnostic amino acid residues can still be correlated to distinct actin genes in fish species.
dc.languageeng
dc.publisherSociedade Brasileira de Genética
dc.relationGenetics and Molecular Biology
dc.relation1.493
dc.relation0,638
dc.rightsAcesso aberto
dc.sourceSciELO
dc.subjectactin gene
dc.subjectamino acid residues
dc.subjectgene structure
dc.subjectNile tilapia
dc.subjectnucleotide sequence
dc.subjectOreochromis niloticus
dc.titlePartial molecular characterization of the Nile tilapia (Oreochromis niloticus) alpha-cardiac muscle actin gene and its relationship to actin isoforms of other fish species
dc.typeArtigo


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