Examination of calf prochymosin accumulation in Escherichia coli: disulphide linkages are a structural component of prochymosin-containing inclusion bodies.
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چکیده
منابع مشابه
Solubilization and activation of recombinant calf prochymosin from Escherichia coli.
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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A gene for calf prochymosin (prorennin) has been reconstructed from chemically synthesized oligodeoxyribonucleotides and cloned DNA copies of preprochymosin mRNA. This gene has been inserted into a bacterial expression plasmid containing the Escherichia coli tryptophan promoter and a bacterial ribosome binding site. Induction of transcription from the tryptophan promoter results in prochymosin ...
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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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Prochymosin (PC) sequence was cloned in Bacillus subtilis using two kinds of plasmid constructions. In plasmid pSM316 the cDNA was inserted to obtain the intracellular expression of the enzyme. The enzyme turned out to be expressed in an insoluble form which could be converted to native enzyme under proper denaturing and refolding conditions. The levels of intracellular expression of PC were fu...
متن کاملAssisted refolding of recombinant prochymosin with the aid of protein disulphide isomerase.
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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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 1985
ISSN: 0261-4189
DOI: 10.1002/j.1460-2075.1985.tb03696.x