[Exposure of cooperativity of the active sites of rabbit skeletal muscle creatine kinase during its interaction with gamma-amides of ATP].
The cooperativity of the active sites of creatine kinase from rabbit skeletal muscle (2.7.3.2) during its interaction with gamma-amides of ATP, e. g. gamma-anilide ATP (I), gamma-benzylamide ATP (II), N-2-hydroxyethyl-N-methyl-gamma-amide ATP (III) and 4-(N-2-hydroxyethyl-N-methylamino)-benzyl-gamma-amide ATP (IV) was studied. A fluorimetric assay of the enzyme complex formation with the analogs was carried out. The values of the intrinsic dissociation constants for the complexes were calculated from the equation for consecutive order of ligands addition. The negative cooperativity of the nucleotide binding sites was found for analogs I and II. Analogs III and IV revealed no noticeable differences in the values of intrinsic dissociation constants. Creatine was shown to have no influence on the cooperativity of the nucleotide binding sites.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D003402:Creatine Kinase / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship
C032381:ATP gamma-anilide; C032382:ATP gamma-benzylamide; C032384:ATP gamma-(4-(N-(2-hydroxyethyl)-N-methylamino)benzylamide); C032383:ATP gamma-(N-(2-hydroxyethyl)-N-methyl)amide; D000255:Adenosine Triphosphate; D003402:Creatine Kinase
Proiavlenie kooperativnosti pri vzaimodeĭstvii kreatinkinazy iz skeletnykh myshts krolika s gamma-amidami-ATP.