小型哺乳动物肌红蛋白的构象自由能

Conformational free energies of myoglobins of small mammals.

作者信息

Kelly L, Simmons J H, Heck T, Holladay L A

机构信息

Department of Chemistry, Louisiana Tech University, Ruston.

出版信息

Int J Pept Protein Res. 1988 Mar;31(3):281-8. doi: 10.1111/j.1399-3011.1988.tb00035.x.

DOI:10.1111/j.1399-3011.1988.tb00035.x

PMID:3372133

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.

摘要

从三种小型胎盘哺乳动物和一种小型有袋动物的心脏或骨骼肌中分离出肌红蛋白。根据pH值为8和25摄氏度时氯化胍展开数据估算这四种肌红蛋白的构象自由能。大鼠和兔子的肌红蛋白比之前研究过的最稳定的肌红蛋白（抹香鲸的肌红蛋白）更稳定。此外，这两种肌红蛋白展开时的协同性比之前表征过的肌红蛋白更高。本文获得的数据首次明确证明，恒温动物肌红蛋白的稳定性与生物体的大小及其代谢率均无关。