Kinetics of assembly and dissociation of the mitochondrial creatine kinase octamer. A fluorescence study.

@article{Gross1993KineticsOA,
  title={Kinetics of assembly and dissociation of the mitochondrial creatine kinase octamer. A fluorescence study.},
  author={Martin Gross and Theo Wallimann},
  journal={Biochemistry},
  year={1993},
  volume={32 50},
  pages={
          13933-40
        }
}
The dissociation of octameric mitochondrial creatine kinase (Mi-CK) into dimers induced by the transition-state analogue complex (TSAC) mixture (creatine+Mg(2+)+ADP+NO3-) is accompanied by a large (25.2%) decrease in Trp fluorescence. This effect is caused by a Trp residue situated at the dimer-dimer interface within the octamer, which becomes susceptible to solvent quenching upon octamer dissociation. Octamer formation, induced by adding excess EDTA to TSAC-dissociated Mi-CK, involves a… CONTINUE READING

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