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Artificial Cell Containing Superoxide Dismutase - Selection of Folding Aids for Stabilisation of Sod

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Artificial Cell Containing Superoxide Dismutase - Selection of Folding Aids for Stabilisation of Sod

Abstract

Superoxide dismutase (abbreviated as SOD) has been vigorously studied in the fields of radical chemistry and related life science. One of practical problems is how to keep its activity in certain adverse conditions causing denaturation. Artificial cell containing SOD can be prepared by polymer encapsulation or nanocapsulation which has been found to be effective to improve the stability of SOD. For construction of an ideal artificial cell system, some folding aids or aggregation inhibitors were utilised to enhance SOD stability. In this study, three groups of biopolymers are selected as folding aids or aggregation inhibitors for stabilisation of SOD, i.e. albumin, carbohydrates and glycoproteins. Results indicate that the thermostability of SOD is affected by different sort of albumin while some carbohydrates such as cyclodextrins are found to be able to enhance SOD stability. In addition, it is firstly found that selected glycoproteins such as alpha-macroglobulin and ovalbumin are several types of effective folding aids for stabilisation of SOD. They can protect SOD against denaturation even at very high temperature(over 100°C). The stability was tested by the measurement of SOD activity loss using auto-oxidation method in different adverse conditions such as high temperature, extreme pH medium, proteolytic hydrolysis and long shelf life storage. The possible stabilisation mechanism of using cyclodextrins and glycoproteins as folding aids were discussed.
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Title
Artificial Cell Containing Superoxide Dismutase - Selection of Folding Aids for Stabilisation of Sod
Author(s)
Zhao, X. B.; Qian, H.; Courtney, J. M.
Journal
Artificial Cells, Blood Substitutes, and Biotechnology , Volume 26 (4) Informa Healthcare – Jan 1, 1998
Publisher
Informa UK Ltd
Copyright
© 1998 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted
Subject
Original Article
ISSN
1073-1199
eISSN
1532-4184
D.O.I.
10.3109/10731199809117676
Publisher site
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