NDLI: The influence of intersubunit cross-linking on the conformational changes of creatine kinase during denaturation by guanidine hydrochloride

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The influence of intersubunit cross-linking on the conformational changes of creatine kinase during denaturation by guanidine hydrochloride

Content Provider	Scilit
Author	Zhu, Li Fan, Ying-Xin Zhou, Jun-Mei
Copyright Year	1997
Description	Intersubunit cross‐linked creatine kinase (CK) has been prepared with the cross‐linking reagent dithiobis(succinimidyl propionate) (DTSP). Unfolding of cross‐linked CK during denaturation by guanidine hydrochloride (GuHC1), as monitored by intrinsic fluorescence, circular dichroism and fluorescence of the hydrophobic probe, 1‐aniline‐naphthalene‐8‐sulfonate (ANS), occurs in two stages with increasing GuHC1 concentration. The process is similar to that of the unmodified enzyme, but in the second stage, conformational changes of the cross‐linked enzyme need higher concentration of GuHC1, suggesting that there is a stable intermediate during its unfolding transition and the intermediate is stabilized by intersubunit cross‐linkage.
Related Links	https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1080/15216549700203981
Ending Page	216
Page Count	10
Starting Page	207
e-ISSN	15216551
DOI	10.1080/15216549700203981
Journal	IUBMB life
Issue Number	1
Volume Number	43
Language	English
Publisher	Informa UK Limited
Publisher Date	1997-09-01
Access Restriction	Open
Subject Keyword	Journal: Iubmb Life Biophysics Creatine Kinase Intersubunit Cross‐linking Protein Unfolding Dissociation Folding Intermediate
Content Type	Text
Resource Type	Article

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