Oxidative refolding of recombinant prochymosin
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چکیده
منابع مشابه
Oxidative refolding of recombinant prochymosin.
The disulphide-coupled refolding of recombinant prochymosin from Escherichia coli inclusion bodies was investigated. Prochymosin solubilized from inclusion bodies is endowed with free thiol groups and disulphide bonds. This partially reduced form undergoes renaturation more efficiently than the fully reduced form, suggesting that some native structural elements existing in inclusion bodies and ...
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Protein disulphide isomerase (PDI) was shown to be able to accelerate the refolding of unfolded recombinant prochymosin and to enhance the overall yield of active protein. Unlike previous reports in this study PDI was found to be active at pH values as high as 11. The coincidence of the similar apparent optimum pH values of uncatalysed and PDI-catalysed reactions suggests that conditions favour...
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Expression of recombinant proteins as inclusion bodies in bacteria is one of the most efficient ways to produce cloned proteins, as long as the inclusion body protein can be successfully refolded. Aggregation is the leading cause of decreased refolding yields. Developments during the past year have advanced our understanding of the mechanism of aggregation in in vitro protein folding. New addit...
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Lah, T., Turk, V. &Pain, R. H. (1984) Biochem. J. 218,601-608 McPhie, P. (1980) J. Biol. Chem. 255,4048-4052 Perlmann, G. E. (1956) Arch. Biochem. Biophys. 65,210-217 Privalov, P. L., Mateo, P. L., Khechinashvili, N. N., Stepanov, V. M. & Revina, L. P. (1981) J. Mol. Biol. 152,445-464 Schlamowitz, M., Peterson, L. V. & Wissler, F. C. (1961) Arch. Biochem. Biophys. 92,58-68 Shewale, J. G. & Tang...
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1. Prochymosin in solution in the presence of 8 M-urea is fully unfolded, as indicated by its fluorescence spectrum, fluorescence quenching behaviour and far-u.v.c.d. spectrum. 2. Equilibrium studies on the unfolding of prochymosin and pepsinogen by urea were carried out at pH 7.5 and pH 9.0. The results indicate that the stabilization energies of the two proteins are identical at pH 7.5, but t...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1999
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3400345