Abstract
Highly purified cAMP-dependent protein phosphokinase from adrenal-cortical tissue contains cAMP-receptor activity. In activating the kinase, cAMP binds to the receptor and causes it to dissociate from its complex with the kinase. The kinase, freed of receptor, is fully activated and no longer stimulable by cAMP. Kinase can be similarly activated by differentially denaturing the receptor with heat. Addition of receptor suppresses kinase activity; this suppression can be overcome by cAMP. After dissociation of receptor, two molecular forms of the activated kinase exist. The cAMP receptor thus functions as a repressor of the protein kinase; binding of cAMP to receptor causes it to dissociate from the kinase, which is then fully activated.
MeSH Terms
Adenine Nucleotides
Adrenal Glands/analysis
Animals
Cattle
Chemical Phenomena
Chemistry
Chromatography, DEAE-Cellulose
Cyclic AMP/pharmacology
Electrophoresis
Hot Temperature
In Vitro Techniques
Phosphorus Isotopes
Phosphotransferases/isolation & purification,pharmacology
Protein Binding
Proteins/isolation & purification,pharmacology
Tritium
Ultracentrifugation
Chemicals
Adenine Nucleotides
Phosphorus Isotopes
Proteins
Tritium
Cyclic AMP
Phosphotransferases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gill G N
Garren L D
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22 references, click to expand
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