[Protein modulator of cyclic nucleotide-dependent protein kinases from the shrimp Palaemon adspersus].
A thermostable protein modulator of cyclic nucleotide-dependent protein kinases was isolated and purified from the tissue of the shrimp Palaemon adspersus. The molecular weight, N-terminal amino acid and amino acid composition of the protein modulator were determined and its effects on cAMP-dependent protein kinase depending on substrate and cation concentrations were investigated. The protein modulator under study is a low molecular weight (15 000) acid protein, pI-435, which exerts both strong activating and inhibitory effects on cAMP-dependent protein kinase in the reactions of phosphorylation of protamine and histones, respectively.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D000242:Cyclic AMP / Q000494:pharmacology; D047908:Intracellular Signaling Peptides and Proteins; D007700:Kinetics; D008970:Molecular Weight; D033541:Palaemonidae / Q000201:enzymology*; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism*; D013379:Substrate Specificity
D000596:Amino Acids; D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; C015482:protein kinase modulator; D000242:Cyclic AMP; D011494:Protein Kinases
Belkovyĭ moduliator tsiklonukeotidzavisimykh proteinkinaz iz tkani krevetki (Palaemon adspersus).