Phosphorylation of endogenous protein in primate kidney. Effects of cyclic AMP.
1. Phosphorylation of endogenous proteins in response to cyclic AMP was assessed in membrane and cytosol from primate kidney. 2. Quantitative studies showed that cAMP significantly increased phosphorylation in baboon kidney membranes; in cytosol there was no effect. 3. Phosphorylation of specific proteins which had been electrophoretically separated showed that five major bands were intensified by cAMP in baboon membranes; in cytosol, three bands were intensified. Similar results were found in normal human kidney. 4. Photoaffinity labelling indicated that a 56 kDa band phosphorylated in cytosol may correspond to the regulatory subunit of type II cAMP-dependent protein kinase.
Laminski
N A
NA
Department of Medical Biochemistry, University of Witwatersrand, Johannesburg, South Africa.
Hammond
K D
KD
Meyers
A M
AM
D000345:Affinity Labels; D000818:Animals; D001345:Autoradiography; D002462:Cell Membrane / Q000378:metabolism; D000242:Cyclic AMP / Q000494:pharmacology*; D003600:Cytosol / Q000378:metabolism; D006801:Humans; D007668:Kidney / Q000187:drug effects* / Q000378:metabolism*; D008970:Molecular Weight; D010215:Papio; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism
D000345:Affinity Labels; D010750:Phosphoproteins; D000242:Cyclic AMP; D011494:Protein Kinases