title: 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.
authors: Department of Chemistry, Louisiana Tech University, Ruston.
authors: L
authors: L
authors: Kelly
authors: J H
authors: JH
authors: Simmons
authors: T
authors: T
authors: Heck
authors: L A
authors: LA
authors: Holladay
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D005260:Female; D019791:Guanidine; D006146:Guanidines; D008786:Metmyoglobin; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis; D009211:Myoglobin / Q000302:isolation & purification; D009893:Opossums; D010920:Placenta / Q000032:analysis; D011247:Pregnancy; D011487:Protein Conformation; D011489:Protein Denaturation; D011821:Raccoons; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D000596:Amino Acids; D006146:Guanidines; D009211:Myoglobin; D008786:Metmyoglobin; D019791:Guanidine