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Article

Achievement of renaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor.

FEBS letters - 4 Apr 1994

Matsubara M, Kurimoto E, Kojima S, Miura K, Sakai T

Abstract excerpt

The pro-sequences of proteases have been considered to be required for the refolding of denatured proteases. However, here we report achievement of almost complete restoration of enzymatic activity of subtilisin BPN' in the absence of its pro-sequence. The presence of 2 M potassium acetate in the folding medium enhanced the refolding efficiency of guanidine hydrochloride (GdnHCl)-denatured subtilisin BPN' by up...

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Identifiers

PMID: 8143876
DOI: 10.1016/0014-5793(94)80499-0

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Achievement of renaturation of subtilisin BPN' by a novel procedure using organic salts and a digestible mutant of Streptomyces subtilisin inhibitor.PMID 8143876Read ↗

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Engineering the independent folding of the subtilisin BPN' prodomain: analysis of two-state folding versus protein stability.Semantic proximity Read ↗

Structural changes leading to increased enzymatic activity in an engineered variant of Bacillus lentus subtilisin.Semantic proximity Read ↗

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