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J. Biol. Chem., Vol. 261, Issue 16, 7236-7241, Jun, 1986
Y Kamisaki, S Saheki, M Nakane, JA Palmieri, T Kuno, BY Chang, SA Waldman and F Murad
The soluble form of guanylate cyclase (EC 4.6.1.2) from rat lung has been
purified to homogeneity by a one-step immunoaffinity chromatographic
procedure. The purified soluble guanylate cyclase has specific activities
of 432 and 49.1 nmol of cyclic GMP formed per min/mg protein with manganese
and magnesium ions as a cofactor, respectively. This represents a
purification of approximately 2,000- fold with a 50% recovery. The native
enzyme has a molecular weight of 150,000 and a Stokes radius of 4.8 nm as
determined on Spherogel TSK- G3000SW gel permeation chromatography. Sodium
dodecyl sulfate- polyacrylamide gel electrophoresis results in two
protein-staining bands with molecular weights of 82,000 and 70,000. The
purified soluble guanylate cyclase was also subjected to native
polyacrylamide gel electrophoresis, isoelectric focusing electrophoresis,
ion exchange chromatography, and GTP-agarose affinity chromatography. These
additional purification procedures confirmed the presence of a single
protein peak coincident with enzyme activity. The two subunits separated on
sodium dodecyl sulfate-polyacrylamide gel electrophoresis were shown to
have different primary structures by immunoblotting with monoclonal and
polyclonal antibodies prepared against purified soluble guanylate cyclase
and by peptide mapping with papain or Staphylococcus aureus V8 protease
treatment. These data demonstrate that soluble guanylate cyclase purified
from rat lung is a heterodimer composed of 82,000- and 70,000-dalton
subunits with different primary structures.
Soluble guanylate cyclase from rat lung exists as a heterodimer
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