Dissociation and unfolding of Pi-class glutathione transferase. Evidence for a monomeric inactive intermediate.

The dissociation and unfolding of the homodimeric glutathione transferase (GST) Pi from human placenta, using different physicochemical denaturants, have been investigated at equilibrium. The protein transitions were followed by monitoring loss of activity, intrinsic fluorescence, tyrosine exposure,...

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Bibliografiske detaljer
Main Authors: Aceto, A, Caccuri, A M, Sacchetta, P, Bucciarelli, T, Dragani, B, Rosato, N, Federici, G, Di Ilio, C
Format: Artigo
Sprog:Inglês
Udgivet: 1992
Fag:
Research Article
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1132772/
https://ncbi.nlm.nih.gov/pubmed/1637306
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