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. 1983 Mar 1;209(3):763–770. doi: 10.1042/bj2090763

The refolding of denatured rabbit muscle pyruvate kinase.

N C Price, E Stevens
PMCID: PMC1154155  PMID: 6870790

Abstract

The refolding of rabbit muscle pyruvate kinase after denaturation by guanidine hydrochloride was studied. On dilution of the denaturing agent, enzyme activity is only partially regained. The extent of regain of activity is dependent on protein concentration, showing a marked decrease at higher concentrations. The failure to regain complete activity appears to be related to the formation of inactive aggregates, which can be separated from active enzyme by gel filtration. Insoluble aggregates can be partially re-activated after solubilization in guanidine hydrochloride. Changes in the circular-dichroism and fluorescence spectra during refolding suggest that a partially folded, inactive species is formed rapidly; this differs from native enzyme in being more susceptible to proteolysis by trypsin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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