Homology between regulatory subunits of type 1 cyclic AMP-dependent protein kinases from bovine and murine cells.
The major cAMP-binding proteins isolated from [35S]methionine-labeled S49 mouse lymphoma cells or MDBK bovine kidney cells correspond in isoelectric point and apparent molecular weight to the regulatory subunit (R) of type I cAMP-dependent protein kinase. These proteins were compared directly by two-dimensional gel electrophoresis and by two-dimensional gel electrophoresis of peptides generated either from native R with thermolysin and chymotrypsin or from denatured R with papain. Both the undigested proteins and all their major peptides were identical in charge and apparent molecular weights, indicating a very high degree of structural homology.
D000818:Animals; D002417:Cattle; D002460:Cell Line; D002918:Chymotrypsin; D000242:Cyclic AMP / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D007668:Kidney; D008223:Lymphoma; D051379:Mice; D008970:Molecular Weight; D010206:Papain; D010446:Peptide Fragments; D011494:Protein Kinases; D013045:Species Specificity; D013820:Thermolysin
D010446:Peptide Fragments; D000242:Cyclic AMP; D011494:Protein Kinases; D002918:Chymotrypsin; D010206:Papain; D013820:Thermolysin