| pubmed-article:3574296 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3574296 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:3574296 | lifeskim:mentions | umls-concept:C0010531 | lld:lifeskim |
| pubmed-article:3574296 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:3574296 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:3574296 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:3574296 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:3574296 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:3574296 | lifeskim:mentions | umls-concept:C0205198 | lld:lifeskim |
| pubmed-article:3574296 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:3574296 | pubmed:dateCreated | 1987-6-18 | lld:pubmed |
| pubmed-article:3574296 | pubmed:abstractText | The interaction of the catalytic subunit of bovine cardiac muscle cAMP-dependent protein kinase with N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide (H-8), the most potent and selective inhibitor toward cyclic nucleotide-dependent protein kinases in the series of isoquinolinesulfonamide derivatives, was studied. The addition of H-8 protected the catalytic subunit of the enzyme in a dose-dependent manner from irreversible inactivation by the ATP analogue p-fluorosulfonylbenzoyl-5'-adenosine (FSBA). The inactivation followed pseudo-first order kinetics and H-8 reduced the steady state constant of inactivation (Ki) without any effect on the first order rate constant (K3). The quantitative binding of H-8 to the enzyme was measured under conditions of thermodynamic equilibrium using a gel filtration method. The catalytic subunit bound approximately 1 mol of drug/mol of protein with apparent half-maximal binding at 1.0 microM drug, whereas the enzyme irreversibly modified by FSBA did not bind the drug, confirming that the enzyme has no site for H-8 in the catalytic subunit other than the active site. The binding studies also showed that H-8 does not require divalent cations such as Mg2+ to bind to the catalytic subunit of the protein kinase. The binding of H-8 to the active site was characterized using FSBA and other affinity labeling reagents which have been postulated to modify residues at or near the active site of the catalytic subunit. H-8 protected the enzyme against inactivation by FSBA and Cibacron Blue F3GA but did not afford any protection against the covalent modification of 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) and 7-chloro-4-nitro-2,1,3-benzoxadiazole (NBD-Cl), suggesting that the binding site of H-8 does not involve the gamma-subsite of the ATP binding site in the catalytic subunit, since DTNB and NBD-Cl are thought to modify the residues complementary to gamma-phosphate of the ATP molecules. | lld:pubmed |
| pubmed-article:3574296 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3574296 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3574296 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3574296 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3574296 | pubmed:month | May | lld:pubmed |
| pubmed-article:3574296 | pubmed:issn | 0026-895X | lld:pubmed |
| pubmed-article:3574296 | pubmed:author | pubmed-author:HidakaHH | lld:pubmed |
| pubmed-article:3574296 | pubmed:author | pubmed-author:HagiwaraMM | lld:pubmed |
| pubmed-article:3574296 | pubmed:author | pubmed-author:InagakiMM | lld:pubmed |
| pubmed-article:3574296 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3574296 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:3574296 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3574296 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3574296 | pubmed:pagination | 523-8 | lld:pubmed |
| pubmed-article:3574296 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:3574296 | pubmed:meshHeading | pubmed-meshheading:3574296-... | lld:pubmed |
| pubmed-article:3574296 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3574296 | pubmed:articleTitle | Specific binding of a novel compound, N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide (H-8) to the active site of cAMP-dependent protein kinase. | lld:pubmed |
| pubmed-article:3574296 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3574296 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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