Comparison of the biochemical and molecular properties of myoglobins from three Biomphalaria species |
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| Authors: | Kádima N Teixeira Jamil S Oliveira Karyne N Souza Juliana de Moura Cristiane A Brito Teofânia HDA Vidigal Alexandre MC Santos Marcelo M Santoro |
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| Institution: | 1. Instituto de Ciências Biológicas, Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Belo Horizonte/MG 31270-901, Brazil;2. Instituto de Ciências Biológicas, Departamento de Zoologia, Universidade Federal de Minas Gerais, Belo Horizonte/MG 31270-901, Brazil;3. Setor de Ciências Biológicas, Departamento de Patologia básica, Universidade Federal do Paraná, Curitiba/PR 81531-980, Brazil;4. Centro de pesquisa René Rachou, Belo Horizonte/MG 30190-002, Brazil;5. Departamento de Ciências Fisiológicas, Universidade Federal do Espírito Santo, Vitória/ES 29040-090, Brazil |
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| 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. |
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