Conformational free energies of myoglobins of small mammals.


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 degrees. 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. Study holds ProTherm entries: 10112, 10113, 10114, 10115 Extra Details: denaturation; guanidinium chloride; mammals;,myoglobin

Submission Details

ID: qf2FpHPv

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:39 p.m.

Version: 1

Publication Details
Kelly L;Simmons JH;Heck T;Holladay LA,Int. J. Pept. Protein Res. (1988) Conformational free energies of myoglobins of small mammals. PMID:3372133
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