Partially folded intermediates during trypsinogen denaturation
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چکیده
منابع مشابه
Partially folded intermediates during trypsinogen denaturation.
The equilibrium unfolding of bovine trypsinogen was studied by circular dichroism, differential spectra and size exclusion HPLC. The change in free energy of denaturation was delta GH2O = 6.99 +/- 1.40 kcal/mol for guanidine hydrochloride and delta GH2O = 6.37 +/- 0.57 kcal/mol for urea. Satisfactory fits of equilibrium unfolding transitions required a three-state model involving an intermediat...
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The denaturation of the dimeric enzyme glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides by guanidine hydrochloride has been studied using enzymatic activity, intrinsic fluorescence, circular dichroism, and light scattering measurements. Equilibrium experiments at 25 degrees C revealed that between 0.9 and 1.2 M denaturant the enzyme underwent a conformational change, exposing tr...
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ژورنال
عنوان ژورنال: Brazilian Journal of Medical and Biological Research
سال: 1999
ISSN: 0100-879X
DOI: 10.1590/s0100-879x1999000600002