Overexpression of dimeric guanylyl cyclase cores of an atrial natriuretic peptide receptor

Biochem Biophys Res Commun. 1991 Oct 31;180(2):538-44. doi: 10.1016/s0006-291x(05)81098-8.

Abstract

Using a bacterial expression system, large amounts of the catalytic core of an atrial natriuretic peptide receptor guanylyl cyclase were produced and purified. After refolding the protein from a buffer containing urea, the enzyme had positively cooperative kinetics with a Hill coefficient, nH = 1.42 +/- 0.08. Size exclusion chromatography and denaturing polyacrylamide gel electrophoresis demonstrated that the enzyme is composed of homodimers with interacting catalytic sites.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Atrial Natriuretic Factor / metabolism
  • Binding Sites
  • Brain / metabolism
  • Chromatography, Gel
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics
  • Guanylate Cyclase / genetics*
  • Guanylate Cyclase / isolation & purification
  • Guanylate Cyclase / metabolism
  • Kinetics
  • Macromolecular Substances
  • Molecular Weight
  • Protein Conformation
  • Protein Denaturation
  • Rats
  • Receptors, Atrial Natriuretic Factor
  • Receptors, Cell Surface / genetics*
  • Receptors, Cell Surface / isolation & purification
  • Receptors, Cell Surface / metabolism
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism

Substances

  • Macromolecular Substances
  • Receptors, Cell Surface
  • Recombinant Proteins
  • Atrial Natriuretic Factor
  • Guanylate Cyclase
  • Receptors, Atrial Natriuretic Factor