A Protein Binding Assay for Adenosine 3':5'-Cyclic Monophosphate
نویسندگان
چکیده
منابع مشابه
A protein binding assay for adenosine 3':5'-cyclic monophosphate.
A simple and sensitive assay for adenosine 3':5'-cyclic monophosphate (cAMP) has been developed that is based on competition for protein binding of the nucleotide, presumably to a cAMP-dependent protein kinase. The nucleotide-protein complex is adsorbed on a cellulose ester filter. Assay conditions are such that a binding constant approaching 10(-9) M is obtained, and the assay is thus sensitiv...
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Binding of cyclic adenosine 3' ,5'-monophosphate (cAMP) by the cAMP receptor protein in crude cell-free extracts of Escherichia coli was characterized. When cell were grown in glucose, binding was inhibited 50% relative to extracts from cells grown with succinate as carbon source . This inhibition could be relieved by dialysis.
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A highly sensitive nanomechanical cantilever sensor assay based on an electrical measurement has been developed for detecting activated cyclic adenosine monophosphate (cyclic AMP)-dependent protein kinase (PKA). Employing a peptide derived from the heat-stable protein kinase inhibitor (PKI), a magnetic bead system was first selected as a vehicle to immobilize the PKI-(5-24) peptide for capturin...
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An abstract ofthis work appeared in 1976. Clin. Res. 24: 456A. (Abstr.) Dr. Broadus' present address is Division of Endocrinology, Department of Internal Medicine, Yale University, New Haven, Conn. 06510. Received for publication 20 April 1976 and in revisedform 13 June 1977. the validity of the measurements and the expressions employed.
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A novel peptide substrate for adenosine 3',5'-cyclic monophosphate-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37), Leu-Arg-Arg-Trp-Ser-Leu-Gly, was synthesized. Phosphorylation of the peptide causes a 20% increase in the peptide fluorescence intensity at 358 nm. Values of Km and kcat for the phosphorylation reaction at pH 7.0 (25 degrees C), were determined to be 2.7 +/-...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1970
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.67.1.305