Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies
نویسندگان
چکیده
منابع مشابه
Unfolding and refolding studies
Equilibrium and kinetic studies of the unfolding-refolding of goat spleen cathepsin B induced by urea are reported. Tryptophan fluorescence and enzyme activity were monitored. The activity of cathepsin B is lost reversibly at 1.2 M-urea. The enzyme unfolds in two main stages, having a stable intermediate (Y) between its native (N) and fully denatured (D) states. Enzyme activity and kinetic stud...
متن کاملRelationship between kinetic and equilibrium folding intermediates of creatine kinase.
Creatine kinase (CK) is a dimeric enzyme important in ATP regeneration in cells where energy demands are high. The folding of CK under equilibrium and transient conditions has been studied in detail and is found to be complex. At equilibrium in 0.8 M GuHCl, 90% of CK molecules are in the form of a partially structured, monomeric intermediate. We exploit this property to measure kinetics of refo...
متن کاملpostnatal studies of bats (pipistrellus kuhlii and miniopterus schreibersii) & histomorphology and histochemistry studies of organs and diseases of (neurergus microspilotus and n. kaiseri)
1. to determine whether difference in birth body mass influenced growth performance in pipistrellus kuhlii we studied a total of 12 captive-born neonates. bats were assigned to two body mass groups: light birth body mass (lbw: 0.89 ± 0.05, n=8) and heavy birth body mass (hbw: 1.35 ± 0.08, n=4). heavier body mass at birth was associated with rapid postnatal growth (body mass and forearm length) ...
Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase.
Protease digestion experiments have been used to characterize the structure of an equilibrium intermediate in the unfolding of creatine kinase (CK) by low concentrations (0.625 M) of guanidine hydrochloride (GdnHCl). Eighteen of the major products of digestion by trypsin, chymotrypsin and endoproteinase Glu-C have been identified by microsequencing after separation by SDS/PAGE and electroblotti...
متن کاملUnfolding kinetics of dimeric creatine kinase measured by stopped-flow small angle X-ray scattering.
The unfolding kinetics of creatine kinase (CK) in various concentrations of urea or guanidine hydrochloride (GuHCl) was investigated by small angle X-ray scattering (SAXS) using synchrotron radiation, and compared with the results obtained by stopped-flow circular dichroism and stopped-flow fluorescence. Using the three methods, the unfolding kinetics of CK fits well to a single exponential fun...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1998
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560071217