Conformational free energies of myoglobins of small mammals
Myoglobins from three small placental mammals and one small marsupial were isolated from cardiac or skeletal muscle. The conformational free energies of these four myoglobins were estimated from guanidinium chloride unfolding data at pH 8 and 25°. The myoglobins from rat and rabbit are more stable t...
| Published in: | International Journal of Peptide and Protein Research |
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| Main Authors: | , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1988
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1111/j.1399-3011.1988.tb00035.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1399-3011.1988.tb00035.x https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3011.1988.tb00035.x |
| Summary: | Myoglobins from three small placental mammals and one small marsupial were isolated from cardiac or skeletal muscle. The conformational free energies of these four myoglobins were estimated from guanidinium chloride unfolding data at pH 8 and 25°. The myoglobins from rat and rabbit are more stable than that of the most stable myoglobin previously studied, that of the sperm whale. In addition, these two myoglobins unfold with greater cooperativity than previously characterized myoglobins. The data obtained herein demonstrate unequivocally for the first time that the stability of homeotherm myoglobins correlates with neither the size of the organism nor its metabolic rate. |
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