Author | Teixeira, Kádima Nayara | |
Author | Jamil S. Oliveira | |
Author | Karyne N. Souza | |
Author | Juliana de Moura | |
Author | Brito, Cristiane A. | |
Author | Vidigal, Teofânia Heloisa Dutra Amorim | |
Author | Santos, Alexandre Martins Costa | |
Author | Santoro, Marcelo Matos | |
Access date | 2023-07-21T18:08:12Z | |
Available date | 2023-07-21T18:08:12Z | |
Document date | 2011 | |
Citation | TEIXEIRA, Kádima Nayara et al. Comparison of the biochemical and molecular properties of myoglobins from three Biomphalaria species. Biochemical Systematics and Ecology, v. 39, n. 4–6, p. 581-586, 2011. doi.org/10.1016/j.bse.2011.04.006 | en_US |
ISSN | 1873-2925 | en_US |
URI | https://www.arca.fiocruz.br/handle/icict/59719 | |
Language | eng | en_US |
Publisher | Elsevier Ltd. | en_US |
Rights | restricted access | en_US |
Title | Comparison of the biochemical and molecular properties of myoglobins from three Biomphalaria species | en_US |
Type | Article | en_US |
DOI | 10.1016/j.bse.2011.04.006 | |
Abstract | Myoglobin is a globin with heme as prosthetic group whose main known biological role is to bind to O2 reversibly. On account of their large diversity, globins from mollusks have contributed to the study of this protein class. The cDNA of the myoglobins from Biomphalaria straminea and Biomphalaria tenagophila, which have a glutamine as distal residue (E7), were constructed and analyzed by bioinformatic tools. Native (not recombinant) myoglobins of these two Biomphalaria species were purified and their experimental molecular mass (about 16 kDa) and pI (about (8.0) were provided. Data analysis showed that these proteins are monomers with the signature for the classic myoglobin fold and they are blocked in amino terminus probably by an acetyl group. Values of the autoxidation rates showed that these myoglobins oxidized slowly. About the primary sequences of the myoglobins, they turned out to be satisfactory to group mollusks in phylogenetic class. (C) 2011 Elsevier Ltd. All rights reserved | en_US |
Affilliation | Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brazil | en_US |
Affilliation | Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brazil | |
Affilliation | Universidade Federal de Minas Gerais Instituto de Ciências Biológicas. Departamento de Zoologia. Belo Horizonte, MG, Brazil | |
Affilliation | Universidade Federal do Paraná. Setor de Ciências Biológicas. Departamento de Patologia básica. Curitiba, PR, Brazil | |
Affilliation | Fundação Oswaldo Cruz. Centro de pesquisa René Rachou. Belo Horizonte, MG, Brazil | |
Affilliation | Universidade Federal de Minas Gerais Instituto de Ciências Biológicas. Departamento de Zoologia. Belo Horizonte, MG, Brazil | |
Affilliation | Universidade Federal do Espírito Santo. Departamento de Ciências Fisiológicas. Vitória, ES, Brazil | |
Affilliation | Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brazil | |
Subject | Autoxidation rate | en_US |
Subject | Biomphalaria | en_US |
Subject | cDNA myoglobin | en_US |
Subject | Haemoprotein | en_US |
Subject | Myoglobin fold | en_US |
Embargo date | 2099-12-31 | |