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Specific Photoaffinity Labeling of the Adenosine 3′:5′-Cyclic Monophosphate Receptor in Intact Ghosts from Human Erythrocytes

By C. Earl Guthrow, Howard Rasmussen, David J. Brunswick and Barry S. Cooperman

Abstract

[(3)H]N(6)-(Ethyl 2-diazomalonyl)-adenosine 3′:5′-cyclic monophosphate is incorporated into intact ghosts from human erythrocytes on photolysis at 253.7 nm. Incorporation is blocked in the presence of adenosine 3′:5′-cyclic monophosphate (cyclic AMP) and does not occur in the absence of irradiation. Sodium dodecyl sulfate disc gel electrophoresis of solubilized ghosts shows that one protein is labeled. The position of this protein on the gel corresponds exactly to that previously found. [J. Biol. Chem. 247, 8145 (1972)] for the endogeneous protein substrate of the endogenous, cyclic AMP-dependent, protein kinase

Topics: Biological Sciences: Biochemistry
Year: 1973
DOI identifier: 10.1073/pnas.70.12.3344
OAI identifier: oai:pubmedcentral.nih.gov:427233
Provided by: PubMed Central
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