Your browser doesn't support javascript.
loading
Cell toxicity by ricin and elucidation of mechanism of Ricin inactivation.
Meneguelli de Souza, L C; Carvalho, L P de; Araújo, J S; Melo, E J T de; Machado, O L T.
Afiliação
  • Meneguelli de Souza LC; Laboratory of Chemistry and Function of Proteins and Peptides - LQFPP, Center for Biosciences and Biotechnology - CBB, State University of Northern Fluminense Darcy Ribeiro (UENF), Av. Alberto Lamego, 2000, ZC, 28035-200 Campos dos Goytacazes, RJ, Brazil.
  • Carvalho LP; Laboratory of Cell and Tissue Biology - LBCT, Center for Biosciences and Biotechnology - CBB, State University of Northern Fluminense Darcy Ribeiro (UENF), Av. Alberto Lamego, 2000, ZC, 28035-200 Campos dos Goytacazes, RJ, Brazil.
  • Araújo JS; Laboratory of Chemistry and Function of Proteins and Peptides - LQFPP, Center for Biosciences and Biotechnology - CBB, State University of Northern Fluminense Darcy Ribeiro (UENF), Av. Alberto Lamego, 2000, ZC, 28035-200 Campos dos Goytacazes, RJ, Brazil.
  • Melo EJT; Laboratory of Cell and Tissue Biology - LBCT, Center for Biosciences and Biotechnology - CBB, State University of Northern Fluminense Darcy Ribeiro (UENF), Av. Alberto Lamego, 2000, ZC, 28035-200 Campos dos Goytacazes, RJ, Brazil.
  • Machado OLT; Laboratory of Chemistry and Function of Proteins and Peptides - LQFPP, Center for Biosciences and Biotechnology - CBB, State University of Northern Fluminense Darcy Ribeiro (UENF), Av. Alberto Lamego, 2000, ZC, 28035-200 Campos dos Goytacazes, RJ, Brazil. Electronic address: olga@uenf.br.
Int J Biol Macromol ; 113: 821-828, 2018 Jul 01.
Article em En | MEDLINE | ID: mdl-29522821
Castor cake is a by-product of the extraction of oil from from seeds of castor plants (Ricinus communis). This by-product contains high levels of proteins, but a toxic protein, ricin, limits its use as an animal feed. Ricin can be efficiently inactivated by treatment with calcium oxide (CaO), which can be evaluated by a cytotoxicity assay using LLC-MK2 cells. The mechanism by which the CaO treatment inactivates ricin, however, is unclear. We report the structural changes responsible for ricin inactivation. Purified ricin was treated with 0.6% CaO and then analyzed by mass spectrometry. This treatment degraded the ricin at preferential sites. The aqueous CaO solution had a pH >12, which preferentially cleaved asparagine residues, followed by glutamine, serine and glycine residues. The alkaline pH affected the tertiary structure of the ricin, cleaving its polypeptide chains and thereby eliminating its cytotoxic activity.
Assuntos
Palavras-chave
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ricina / Citotoxinas Limite: Animals Idioma: En Revista: Int J Biol Macromol Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ricina / Citotoxinas Limite: Animals Idioma: En Revista: Int J Biol Macromol Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda