Conformational free energies of myoglobins of small mammals
| Autor: | Leslie A. Holladay, Lenore Kelly, Joe H. Simmons, Terry Heck |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
inorganic chemicals
Guanidinium chloride Protein Denaturation Hemeprotein Protein Conformation Placenta Cooperativity Biochemistry Guanidines Chromatography DEAE-Cellulose chemistry.chemical_compound Pregnancy Animals Denaturation (biochemistry) Amino Acids Guanidine Myoglobin Muscles Rats Inbred Strains Opossums Rats Molecular Weight chemistry biological sciences Metabolic rate Chromatography Gel Free energies Female Raccoons Metmyoglobin |
| Zdroj: | International journal of peptide and protein research. 31(3) |
| ISSN: | 0367-8377 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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