PRESENCE OF SITES FOR INTERACTING WITH CYCLIC-AMP AND WITH CATALYTIC SUBUNIT ON SMALL FRAGMENTS OF PROTEIN-KINASE REGULATORY SUBUNIT
- 1 January 1978
- journal article
- research article
- Vol. 253 (6) , 1752-1755
Abstract
During the purification of cyclic[c]AMP binding proteins from rat liver, smaller active fragments were obtained, possibly as the result of proteolysis. The binding proteins detected had approximate MW of 50,000, 36,000 and 10,000. Each of these components bound [3H] cAMP with high affinity (apparent Kd ranging from 2-10 nM) and had a similar ability to inhibit the purified catalytic subunit of rat liver protein kinase. cAMP prevented this inhibition in each instance. The binding site for cAMP and the site for interacting with catalytic subunit occur relatively close to one another on the regulatory subunit and can remain functional when a substantial fraction of the subunit is lost.This publication has 9 references indexed in Scilit:
- Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductasesPublished by Elsevier ,2003
- Study of autophosphorylation of isoenzymes of cyclic AMP-dependent protein kinases.Journal of Biological Chemistry, 1977
- Identification, characterization, and quantitative measurement of cyclic AMP receptor proteins in cytosol of various tissues using a photoaffinity ligand.Journal of Biological Chemistry, 1977
- Purification and characterization of catalytic subunit of skeletal muscle adenosine 3':5'-monophosphate-dependent protein kinase.Journal of Biological Chemistry, 1977
- Mechanism of self-phosphorylation of adenosine 3':5'-monophosphate-dependent protein kinase from bovine cardiac muscle.Journal of Biological Chemistry, 1976
- Adenosine 3':5'-cyclic monophosphate-binding proteins in bovine and rat tissuesBiochemical Journal, 1976
- Purification and characterization of the catalytic subunit of adenosine 3':5'-cyclic monophosphate-dependent protein kinase from bovine liverBiochemical Journal, 1976
- Dissociation and reassociation of the phosphorylated and nonphosphorylated forms of adenosine 3':5' -monophosphate-dependent protein kinase from bovine cardiac muscle.Journal of Biological Chemistry, 1976
- A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein MixturesJournal of Biological Chemistry, 1961