S-pegylthiopapain, a versatile intermediate for the preparation of the fully active form of the cysteine proteinase archetype

Papain is widely used in several laboratories as a reference enzyme and, as such, needs to be highly pure. A one-step purification of the enzyme is described here starting from spray-dried papaya latex. After protection of the essential SH group with a monomethoxypolyethylene glycol derivative synth...

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Bibliographic Details
Published in:Journal of Chromatography A 1996-02, Vol.724 (1), p.185-192
Main Authors: Azarkan, Mohamed, Wintjens, RenéT., Smolders, Nicole, Nijs, Michelle, Looze, Yvan
Format: Article
Language:English
Subjects:
Enzymes
Papain
S-Pegylthiopapain
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Summary:Papain is widely used in several laboratories as a reference enzyme and, as such, needs to be highly pure. A one-step purification of the enzyme is described here starting from spray-dried papaya latex. After protection of the essential SH group with a monomethoxypolyethylene glycol derivative synthesised in our laboratory, the mixture of papaya enzymes is submitted to fractionation on S-Sepharose Fast Flow. This procedure leads to the isolation of the S-pegylthiopapain conjugate devoid of any contamination nor by the enzyme's irreversibly oxidized form nor by one of the other proteinases present in the original mixture. Thereafter, S-pegylthiopapain may be quite easily converted into its fully active form.
ISSN:0021-9673
DOI:10.1016/0021-9673(95)00910-8