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Refolding parameters for the allosteric homodimeric guanylyl cyclase catalytic core from the atrial natriuretic peptide receptor.

Abstract：

: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 microM concentration of substrate. Additional factors are described in this unusual case of renaturing an allosteric homodimeric enzyme in vitro.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Thorpe DS,Niu S,Morkin E

doi

10.1006/bbrc.1996.1097

subject

Has Abstract

pub_date

1996-07-25 00:00:00

pages

765-71

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)91097-9

journal_volume

224

pub_type

杂志文章

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