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Molecular Chaperone-Like Activity of Hydrogel Nanoparticles of Hydrophobized Pullulan: Thermal Stabilization with Refolding of Carbonic Anhydrase B
- Source :
- Bioconjugate Chemistry; May 17, 1999, Vol. 10 Issue: 3 p321-324, 4p
- Publication Year :
- 1999
-
Abstract
- We have been studying the formation of hydrogel nanoparticles by the self-aggregation of hydrophobized polysaccharide and the effective complexation between these nanoparticles as a host and various globular soluble proteins as a guest. This paper describes a new finding that refolding of the heat-denatured enzyme effectively occurs with the nanoparticles and β-cyclodextrin according to a mechanism similar to that of a molecular chaperone. In particular, the irreversible aggregation of carbonic anhydrase B (CAB) upon heating was completely prevented by complexation between the heat-denatured enzyme and hydrogel nanoparticles formed by the self-aggregation of cholesteryl group-bearing pullulan (CHP). The complexed CAB was released by dissociation of the self-aggregate upon the addition of β-cyclodextrin. The released CAB refolded to the native form, and almost 100% recovery of the activity was achieved. The thermal stability of CAB was drastically improved by capture of the unfolded form which was then released to undergo refolding.
Details
- Language :
- English
- ISSN :
- 10431802 and 15204812
- Volume :
- 10
- Issue :
- 3
- Database :
- Supplemental Index
- Journal :
- Bioconjugate Chemistry
- Publication Type :
- Periodical
- Accession number :
- ejs1059842