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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Atrial Natriuretic Factor / metabolism
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Binding Sites
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Brain / metabolism
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Chromatography, Gel
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Cloning, Molecular
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / genetics
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Guanylate Cyclase / genetics*
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Guanylate Cyclase / isolation & purification
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Guanylate Cyclase / metabolism
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Kinetics
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Macromolecular Substances
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Molecular Weight
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Protein Conformation
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Protein Denaturation
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Rats
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Receptors, Atrial Natriuretic Factor
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Receptors, Cell Surface / genetics*
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Receptors, Cell Surface / isolation & purification
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Receptors, Cell Surface / metabolism
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
Substances
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Macromolecular Substances
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Receptors, Cell Surface
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Recombinant Proteins
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Atrial Natriuretic Factor
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Guanylate Cyclase
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Receptors, Atrial Natriuretic Factor