Purification and characterization of a specific late-larval esterase from two species of the Drosophila repleta group: contributions to understand its evolution (2014)
- Authors:
- Autor USP: CABRAL, HAMILTON - FCFRP
- Unidade: FCFRP
- DOI: 10.1186/1810-522X-53-6
- Assunto: BIOQUÍMICA (EVOLUÇÃO)
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Zoological Studies
- ISSN: 1021-5506
- Volume/Número/Paginação/Ano: v. 53, art. 6, 2014
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: hybrid
- Licença: cc-by
-
ABNT
LOPES, Vanessa F. et al. Purification and characterization of a specific late-larval esterase from two species of the Drosophila repleta group: contributions to understand its evolution. Zoological Studies, v. 53, 2014Tradução . . Disponível em: https://doi.org/10.1186/1810-522X-53-6. Acesso em: 19 abr. 2024. -
APA
Lopes, V. F., Cabral, H., Machado, L. P. B., & Mateus, R. P. (2014). Purification and characterization of a specific late-larval esterase from two species of the Drosophila repleta group: contributions to understand its evolution. Zoological Studies, 53. doi:10.1186/1810-522X-53-6 -
NLM
Lopes VF, Cabral H, Machado LPB, Mateus RP. Purification and characterization of a specific late-larval esterase from two species of the Drosophila repleta group: contributions to understand its evolution [Internet]. Zoological Studies. 2014 ; 53[citado 2024 abr. 19 ] Available from: https://doi.org/10.1186/1810-522X-53-6 -
Vancouver
Lopes VF, Cabral H, Machado LPB, Mateus RP. Purification and characterization of a specific late-larval esterase from two species of the Drosophila repleta group: contributions to understand its evolution [Internet]. Zoological Studies. 2014 ; 53[citado 2024 abr. 19 ] Available from: https://doi.org/10.1186/1810-522X-53-6 - Partial purification and characterization of protease from thermophilic fungus, thermomyces lanuginosus, and its hydrolytic activity on milk proteins
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Informações sobre o DOI: 10.1186/1810-522X-53-6 (Fonte: oaDOI API)
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