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Purification, Biochemical and Functional Characterization of Miliin, a New Thiol-Dependent Serine Protease Isolated from the Latex of Euphorbia milii

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Abstract:

Miliin, a new thiol-dependent serine protease purified from the latex of Euphorbia milii possesses a molecular weight of 79 kDa, an isoelectric point of 4.3 and is optimally active at 60 °C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease.





Keywords: Characterization; Euphorbia milii; Latex; Medicinal plant; Purification; Serine protease

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986608785133744

Publication date: July 1, 2008

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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