Refolding of urea-denatured adenylate kinase
نویسندگان
چکیده
منابع مشابه
The refolding of denatured rabbit muscle pyruvate kinase.
The refolding of rabbit muscle pyruvate kinase after denaturation by guanidine hydrochloride was studied. On dilution of the denaturing agent, enzyme activity is only partially regained. The extent of regain of activity is dependent on protein concentration, showing a marked decrease at higher concentrations. The failure to regain complete activity appears to be related to the formation of inac...
متن کاملRefolding of denatured and denatured/reduced lysozyme at high concentrations.
Refolding of proteins at high concentrations often results in aggregation. To gain insight into the molecular aspects of refolding and to improve the yield of active protein, we have studied the refolding of lysozyme either from its denatured state or from its denatured/reduced state. Refolding of denatured lysozyme, even at 1 mg/ml, yields fully active enzyme without aggregation. However, refo...
متن کاملStable intermediates can be trapped during the reversible refolding of urea-denatured rhodanese.
The enzyme rhodanese (EC 2.8.1.1) could be reversibly refolded from urea in the presence of lauryl maltoside, beta-mercaptoethanol, and sodium thiosulfate. The unfolding/folding transition monitored using intrinsic fluorescence was resolved into two two-state transitions with midpoints at 3.6 and 5.0 M urea. The analysis assumed an intermediate with an emission maximum at 345 nm. Monitoring ani...
متن کاملThe refolding of denatured rabbit muscle creatine kinase. Search for intermediates in the refolding process and effect of modification at the reactive thiol group on refolding.
A number of aspects of the refolding of denatured rabbit muscle creatine kinase have been studied. Addition of substrates has no effect on the rate or extent of regain of activity. The changes in protein fluorescence during refolding broadly parallel the regain of activity. A study of the susceptibility of the enzyme to proteolysis during refolding indicates that there is no significant accumul...
متن کاملSynthetic "chaperones": nanoparticle-mediated refolding of thermally denatured proteins.
Thermally denatured chymotrypsin, lysozyme and papain are substantially refolded towards their native conformation by gold nanoparticle bearing dicarboxylate sidechains.
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1998
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3330401