Assisted refolding of recombinant prochymosin with the aid of protein disulphide isomerase
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چکیده
منابع مشابه
Assisted 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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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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What is it? Protein disulphide isomerase is an enzyme with two interrelated activities: as an oxidoreductase, it can catalyse the formation, reduction and isomerisation of disulphide bonds; and as a polypeptide binding protein, it can function as a molecular chaperone which assists the folding of polypeptides. Transient association of PDI with nascent polypeptides during their folding prevents ...
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Disulphide bonds are found in practically every class of extracellular protein, and the formation of disulphide bonds must be regarded as a key post-translational modification of secretory proteins. Despite this, and despite the fact that the existence of disulphide bonds has been known for many years, the mechanism of disulphide bond formation during protein biosynthesis and secretion is not w...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1994
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3010017