Reactivation of 3-phosphoglycerate kinase from its unfolded proteolytic fragments.

@article{Vas1990ReactivationO3,
  title={Reactivation of 3-phosphoglycerate kinase from its unfolded proteolytic fragments.},
  author={M{\'a}ria Vas and Michael A. Sinev and Natalia V. Kotova and Gennady V. Semisotnov},
  journal={European journal of biochemistry},
  year={1990},
  volume={189 3},
  pages={575-9}
}
Limited trypsinolysis of pig muscle 3-phosphoglycerate kinase yielded a nicked enzyme without loss of catalytic activity [Jiang, S. X. & Vas, M. (1988) FEBS Lett. 231, 151-154]. The reactivation rate of the nicked enzyme after denaturation does not differ substantially from the reactivation rate of the denatured intact enzyme: t 1/2 varies between 70-110 s at 25 degrees C, pH 7.0 in both cases. Thus, the absence of a covalent linkage between the two proteolytic fragments of the enzyme molecule… CONTINUE READING

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