Kinetics of unfolding of dogfish muscle lactate dehydrogenase in the presence of guanidine hydrochloride

Paul M. Wassarman, John W. Burgner

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish
Pages (from-to)537-542
Number of pages6
JournalJournal of Molecular Biology
Volume67
Issue number3
DOIs
StatePublished - 28 Jun 1972
Externally publishedYes

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