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Conformational free energies of myoglobins of small mammals |
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| Authors: | LENORE KELLY JOE H SIMMONS TERRY HECK LESLIE A HOLLADAY |
| Institution: | 1. Department of Chemistry, Louisiana Tech University, Ruston, LA, USA
Current address: Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.;2. Department of Chemistry, Louisiana Tech University, Ruston, LA, USA A portion of this work was abstracted from the M.S. thesis of T.H.;3. Department of Chemistry, Louisiana Tech University, Ruston, LA, USA |
| Abstract: | 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. |
| Keywords: | denaturation guanidinium chloride mammals myoglobin |