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- W1966628077 abstract "The refolding of urea-denatured ribonuclease A was measured at 0.31–3.1 mol · l−1 urea in the presence of various concentrations of peptidyl-prolyl cis-trans isomerase isolated from pig kidney. The rate of the slow CT-phase in the refolding reaction was found to be sensitive to this enzyme. A rate enhancement proportional to the isomerase activity has been observed. The activity of the enzyme was assayed with Glt-Ala-Ala-Pro-Phe-4-nitroanilide. The catalytic activity of the isomerase against unfolded ribonuclease is suppressed after preincubation of the enzyme with 0.001 mol · l−1 Cuḃ+, 0.01 mol · l−1 H+ and by heat inactivation. The results indicate the involvement of the cis/trans interconversion of proline peptide bonds during the refolding of ribonuclease A." @default.
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- W1966628077 date "1985-03-01" @default.
- W1966628077 modified "2023-10-12" @default.
- W1966628077 title "The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase" @default.
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- W1966628077 doi "https://doi.org/10.1016/0167-4838(85)90006-8" @default.
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