Purification and properties of the cyclic 3',5'-AMP-binding protein from the muscle of the Nematode Ascaris suum.
The cyclic 3',5'-AMP-binding protein was isolated from the muscle of Ascaris suum and purified to apparent homogeneity. It migrated as a protein with a relative Mr 54,000 on electrophoresis under denaturing conditions. On gel filtration columns it was eluted at a volume corresponding to a protein of Mr greater than 200,000 under conditions which kept the cyclic 3',5'-AMP-binding property intact. The purified catalytic subunit of protein kinase from Ascaris and the C subunit of cyclic 3',5'-AMP-dependent protein kinase from bovine heart were inhibited by the cyclic 3',5'-AMP-binding protein. Gel filtration studies indicated the formation of a stable protein complex between the protein kinase and the cyclic 3',5'-AMP-binding protein from Ascaris.
Thalhofer
H P
HP
Faculty of Biology, University of Konstanz, Federal Republic of Germany.
Starz
W
W
Daum
G
G
Wurster
B
B
Harris
B G
BG
Hofer
H W
HW
D000818:Animals; D001200:Ascaris / Q000032:analysis*; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D000242:Cyclic AMP / Q000494:pharmacology; D002373:Cyclic AMP Receptor Protein; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis; D009206:Myocardium / Q000201:enzymology; D047428:Protein Kinase Inhibitors
D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D047428:Protein Kinase Inhibitors; D000242:Cyclic AMP