Characterization and partial purification of a membrane protein from rabbit skeletal muscle which inhibits the cAMP-dependent protein kinase.
Rabbit skeletal muscle membranes contain a protein which inhibits the cAMP-dependent protein kinase. The activity of the partially purified membrane protein is characterized by an IC-50 of 10 to 30 nM with respect to the inhibition of the activity of the catalytic subunit of the cAMP-dependent protein kinase and is sensitive to treatment with heat, acid, alkali and trypsin. The active fractions contain proteins ranging from 40 to 120 kDa, analysed by SDS-gel electrophoresis.
Woscholski
R
R
Institute of Molecular Cell Biology, University of Freiburg, Germany.
Marmé
D
D
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D047908:Intracellular Signaling Peptides and Proteins; D007700:Kinetics; D008565:Membrane Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D009132:Muscles / Q000502:physiology*; D047428:Protein Kinase Inhibitors; D011817:Rabbits
D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D047428:Protein Kinase Inhibitors; C015482:protein kinase modulator