Refolding parameters for the allosteric homodimeric guanylyl cyclase catalytic core from the atrial natriuretic peptide receptor.
Refolding parameters for the allosteric homodimeric guanylyl cyclase catalytic core from the atrial natriuretic peptide receptor.
复制标题
心房钠尿肽受体变构同二聚鸟苷酸环化酶催化核心的重折叠参数。
DOI：
10.1006/bbrc.1996.1097
复制
发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Morkin,E
中科院分区：
文献类型：
--
作者：
Thorpe,DS;Niu,S;Morkin,E
Protein folding continues to be an important biophysical topic in molecular biology. We report the parameters for successfully refolding the guanylyl cyclase core of the ANP receptor, an allosteric homodimeric enzyme. Urea was a better chaotropic solvent than guanidine HCl, and physiological salt concentrations and pH were needed for optimal recovery of enzymatic activity. Renaturation was more sensitive to alkaline compared to acidic deviations in solvent conditions. The time course of refolding was sigmoidal producing an enzyme with a specific activity of 16,000 pmol cGMP/min/mg using 60 μM concentration of substrate. Additional factors are described in this unusual case of renaturing an allosteric homodimeric enzymein vitro.
