Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii

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Data

2008-07-01

Autores

Moro, L. P. [UNESP]
Murakami, M. T.
Cabral, Hamilton [UNESP]
Vidotto, A.
Tajara, E. H.
Arni, R. K. [UNESP]
Juliano, L.
Bonilla-Rodriguez, Gustavo Orlando [UNESP]

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ISSN da Revista

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Editor

Bentham Science Publ Ltd

Resumo

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 degrees C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease.

Descrição

Palavras-chave

Medicinal plant, latex, Euphorbia milii, serine protease, Purification, Characterization

Como citar

Protein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 15, n. 7, p. 724-730, 2008.