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- W2041016686 abstract "Abstract Dogfish muscle lactate dehydrogenase was found to contain 7.0 (± 0.2) sulfhydryl groups per polypeptide chain (35,000 mol.-wt), of which 1.9 (± 0.2) are free to react with 5,5′-dithiobis(2-nitrobenzoic acid) in the native enzyme. The reaction of the five “masked” sulfhydryl groups with this reagent has been used to measure the rate of unfolding of lactate dehydrogenase as a function of guanidine hydrochloride concentration. The results are compatible with a one-step denaturation process involving a transition between native and completely unfolded molecules without the accumulation of stable intermediates." @default.
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- W2041016686 title "Kinetics of unfolding of dogfish muscle lactate dehydrogenase in the presence of guanidine hydrochloride" @default.
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- W2041016686 doi "https://doi.org/10.1016/0022-2836(72)90473-1" @default.
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