ISSN: 2329-9053

Journal of Molecular Pharmaceutics & Organic Process Research
Open Access

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In-vitro refolding of recombinant human (rh) Prolidase using smart polymer

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Copyright: © 2020  . This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 
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Abstract

Statement of the Problem: A member of the metallopeptidase family, Prolidase is an exopeptidase involved in the final steps of the catabolism of proline-rich and hydroxyproline-rich dietary and endogenous proteins such as collagen. Mutations in the gene encoding for prolidase brings about autosomal recessive prolidase deficiency characterized by intractable ulcerations in the skin, varied extent of mental retardation and recurrent infections of the respiratory tract. Prolidase has additionally been known to function similar to organophosphorus acid anhydrolase in hydrolyzing organophosphorus compounds

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