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

Artículos de revistas

Fecha

2008-07-01

Registro en:

Protein and Peptide Letters, v. 15, n. 7, p. 724-730, 2008.

0929-8665

http://hdl.handle.net/11449/225247

10.2174/092986608785133744

2-s2.0-49449115536

https://repositorioslatinoamericanos.uchile.cl/handle/2250/5405377

Autor

Universidade Estadual Paulista (UNESP)

Laboratory

Universidade de São Paulo (USP)

FAMERP

Universidade Federal de São Paulo (UNIFESP)

Institución

Universidade Estadual Paulista (Brasil)

Resumen

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. © 2008 Bentham Science Publishers Ltd.

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Latex

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