Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii
| Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
|---|---|
| Data(s) |
20/05/2014
20/05/2014
01/07/2008
|
| 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. |
| Formato |
724-730 |
| Identificador |
http://eurekaselect.com/83070/article Protein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 15, n. 7, p. 724-730, 2008. 0929-8665 http://hdl.handle.net/11449/22025 WOS:000259509600012 |
| Idioma(s) |
eng |
| Publicador |
Bentham Science Publ Ltd |
| Relação |
Protein and Peptide Letters |
| Direitos |
closedAccess |
| Palavras-Chave | #Medicinal plant #latex #Euphorbia milii #serine protease #Purification #Characterization |
| Tipo |
info:eu-repo/semantics/article |
