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- W2025021649 abstract "Reconstitution of tetrameric lactic dehydrogenase from pig muscle after maximum unfolding in 6M guanidine · HCI produces about equal amounts of native enzyme and inactive aggregates. The decrease in the recon‐ stitution capacity is not determined by chemical modification or aggregation in the denatured state. Instead, a kinetic competition between refolding and aggregation during reconstitution must be assumed, similar to the mechanism proposed earlier for the reconstitution after acid dissociation; under this condition conformational rearrangements within residual structures of the acid‐dissociated state were found to be decisive for the decrease in rate and yield of reactivation [G. Zettlmeißl et al. (1979) Biochemistry, 18 , 5567‐5571; (1981) Eur. J. Binchem. 121 , 169‐1751. To determine whether the yield of reactivation after dissociation and denaturation by guanidine · HCl is influenced by proline cis ⇋ trans isomerization in the denatured state [cf. J. F. Brandts et al. (1975) Biochemistry, 14 , 4953‐49631, time‐dependent measurements were performed. Unfolding in 6 M guanidine · HCI as determined by the decrease in protein fluorescence is found to be very fast (τ= 18.7 ms at 20 °C). Aggregation occurs even after very short times of denaturation where all X‐proline peptide bonds of the denatured chains are expected still to be in their native isomeric conformation. Therefore, the ratio of aggregation and reactivation is not likely to be determined by proline cis trans isomerism. As indicated by the independence of the rate of reactivation on the isomerization state of proline, the slow folding reaction on the correct first‐order/second‐order pathway of reactivation must be determined by rate‐limiting steps other than proline isomerism." @default.
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- W2025021649 date "1982-07-01" @default.
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- W2025021649 title "The Yield of Reactivation of Lactic Dehydrogenase after Guanidine · HCl Denaturation is Not Determined by Proline<i>cis</i>⇋<i>trans</i>Isomerization" @default.
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- W2025021649 doi "https://doi.org/10.1111/j.1432-1033.1982.tb06725.x" @default.
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