The Saturation Assay of Adenosine 3′:5′-Cyclic Monophosphate in Tissues and Body Fluids

Brown, Barry L.; Albano, J. D. M.; Barnes, Godfrey; Ekins, Roger

doi:10.1042/bst0020388

Cited by 12 publications

(2 citation statements)

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“…For both intracellular and extracellular samples. cyclic AMP was assayed as described previously (Brown et al, 1971(Brown et al, , 1974. Material that was assayed as cAMP was destroyed in the same way as bonafide cAMP by beef heart phosphodiesterase.…”

Section: Elutriutionmentioning

confidence: 99%

Intracellular and extracellular levels of cyclic AMP during the cell cycle of Saccharomyces cerevisiae

Smith

Dickinson

Wheals

1990

Yeast

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Using the technique of centrifugal elutriation it was demonstrated that during the cell division cycle of the budding yeast Saccharomyces cerevisiae there are stage-specific fluctuations in the intracellular concentration of adenosine 3',5'-cyclic monophosphate (cAMP). Results shown here indicate that the intracellular concentration of cAMP is at its highest during the division cycle, and at its lowest immediately prior to and just after cell separation. Results also show the extrusion of extracellular cAMP into the medium by Saccharomyces cerevisiae, extracellular cAMP levels being ten to one hundred times higher than intracellular levels. During the cell cycle of Saccharomyces cerevisiae the extracellular level of cAMP does not fluctuate.

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Section: Elutriutionmentioning

confidence: 99%

Intracellular and extracellular levels of cyclic AMP during the cell cycle of Saccharomyces cerevisiae

Smith

Dickinson

Wheals

1990

Yeast

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“…However, Erlichman, Rosenfeld & Rosen (1974) and Rangel-Aldao & Rosen (1976), also using the protein kinase of cardiac tissue, found no change in the cyclic AMP binding characteristics after autophosphorylation. Furthermore, despite the fact that observed competition for cyclic AMP binding sites by ATP, ADP and AMP at concentrations above 2-4 x 10-7 mol/1, Brown, Albano, Barnes & Ekins (1973) state that their assay, which also uses the bovine adrenal cortex binding protein, is sensitive enough to allow a 1:10 dilution of sample before cyclic AMP assay, thus eliminating interference by enzyme assay com-ponents. Albano, Maudsley, Brown & Barnes (1973) used this assay to study adenylate cyclase in kidney, pituitary and adrenal tissue of the rat.…”

Section: Introductionmentioning

confidence: 94%

Use of a Competitive Protein-Binding Assay for Adenosine 3′:5′-Phosphate for the Study of Bovine Corpus Luteum Adenylate Cyclase

Young¹,

Stansfield²

1977

Journal of Endocrinology

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The use of a competitive protein-binding assay for cyclic AMP, utilizing the binding protein purified from bovine adrenal cortex, for the study of adenylate cyclase activity of the washed 600 g sediment of bovine corpus luteum is validated. A specific assay for cyclic AMP could only be achieved by removal of the degradation products of ATP on a precipitate of nascent BaSO4. Simple dilution of the sample before assay was not sufficient to eliminate interference from degradation products of ATP. An observed variability in optimal ATP substrate and tissue concentrations is though to reflect variability in the enzymic profile of the cyclic corpus luteum. Optima with respect to F-, Mg2+ and pH are more clearly defined and are similar to those reported for adenylate cyclase systems for other tissues.

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The Assay of Cyclic AMP in Biological Material

Brown

Albano

Barnes

et al. 1976

Eukaryotic Cell Function and Growth

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The Saturation Assay of Adenosine 3′:5′-Cyclic Monophosphate in Tissues and Body Fluids

Cited by 12 publications

References 0 publications

Intracellular and extracellular levels of cyclic AMP during the cell cycle of Saccharomyces cerevisiae

Intracellular and extracellular levels of cyclic AMP during the cell cycle of Saccharomyces cerevisiae

Use of a Competitive Protein-Binding Assay for Adenosine 3′:5′-Phosphate for the Study of Bovine Corpus Luteum Adenylate Cyclase

The Assay of Cyclic AMP in Biological Material

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