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- W2012644368 abstract "A simple and sensitive competitive protein-binding assay for cyclic GMP (cGMP) has been developed, using a specific cGMP-binding protein isolated from rat lungs. The contamination of cAMP-binding protein was partially removed by fractionated precipitation with ammonium sulfate. The most active binding was observed when cGMP-binding protein was extracted with phosphate buffer (50 mM) containing 2-mercaptoethanol. Magnesium (40 mM) and zinc (4 and 40 mM) ions enhanced the binding of cGMP to the protein. The amount of protein which bound to cGMP decreased when the protein was extracted with buffer but without 2-mercaptoethanol. The binding constant of this protein was 5.5–16.3 × 10−9 M. The sensitivity of the assay was 0.2 picomole of cGMP. Other nucleotides exerted little or no interference." @default.
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- W2012644368 date "1975-11-01" @default.
- W2012644368 modified "2023-09-25" @default.
- W2012644368 title "A simple and sensitive competitive protein-binding assay for cyclic GMP" @default.
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- W2012644368 doi "https://doi.org/10.1016/0006-291x(75)90839-6" @default.
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