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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/22025
Title: 
Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii
Author(s): 
Institution: 
  • Universidade Estadual Paulista (UNESP)
  • Ctr Struct Mol Biol
  • Universidade de São Paulo (USP)
  • Faculdade de Medicina de São José do Rio Preto (FAMERP)
  • Universidade Federal de São Paulo (UNIFESP)
ISSN: 
0929-8665
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 degrees C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease.
Issue Date: 
1-Jul-2008
Citation: 
Protein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 15, n. 7, p. 724-730, 2008.
Time Duration: 
724-730
Publisher: 
Bentham Science Publ Ltd
Keywords: 
  • Medicinal plant
  • latex
  • Euphorbia milii
  • serine protease
  • Purification
  • Characterization
Source: 
http://eurekaselect.com/83070/article
URI: 
Access Rights: 
Acesso restrito
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/22025
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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