Phosphorus nuclear-magnetic-resonance studies of the transition-state analogue complex of creatine kinase.
31P nuclear-magnetic-resonance spectra of MgADP bound to creatine kinase in the presence of creatine NO3- ions show that there are two non-identical forms of the bound nucleotide. The sites have different affinities for the nucleotide. MgADP at the high-affinity site is in slow exchange (k less than 125s-1 at 27 degrees C) with free MgADP.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D003402:Creatine Kinase / Q000378:metabolism*; D008274:Magnesium / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D011817:Rabbits
D000244:Adenosine Diphosphate; D003402:Creatine Kinase; D008274:Magnesium