Refolding and purification of the human secreted group IID phospholipase 'A IND. 2' expressed as inclusion bodies in escherichia coli (2009)
- Authors:
- USP affiliated author: WARD, RICHARD JOHN - FFCLRP
- School: FFCLRP
- DOI: 10.1016/j.pep.2009.04.006
- Subjects: ESCHERICHIA COLI; FOSFOLIPASES A; HIDRÓLISE
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Protein Expression and Purification
- ISSN: 1046-5928
- Volume/Número/Paginação/Ano: v. 67, n. 2, p. 82-87
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: hybrid
- Licença: implied-oa
-
ABNT
FONSECA, Raquel Gomes; FERREIRA, Tatiana Lopes; WARD, Richard John. Refolding and purification of the human secreted group IID phospholipase 'A IND. 2' expressed as inclusion bodies in escherichia coli. Protein Expression and Purification, San Diego, v. 67, n. 2, p. 82-87, 2009. DOI: 10.1016/j.pep.2009.04.006. -
APA
Fonseca, R. G., Ferreira, T. L., & Ward, R. J. (2009). Refolding and purification of the human secreted group IID phospholipase 'A IND. 2' expressed as inclusion bodies in escherichia coli. Protein Expression and Purification, 67( 2), 82-87. doi:10.1016/j.pep.2009.04.006 -
NLM
Fonseca RG, Ferreira TL, Ward RJ. Refolding and purification of the human secreted group IID phospholipase 'A IND. 2' expressed as inclusion bodies in escherichia coli. Protein Expression and Purification. 2009 ; 67( 2): 82-87. -
Vancouver
Fonseca RG, Ferreira TL, Ward RJ. Refolding and purification of the human secreted group IID phospholipase 'A IND. 2' expressed as inclusion bodies in escherichia coli. Protein Expression and Purification. 2009 ; 67( 2): 82-87. - Relação estrutura/ função de proteínas
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- Crystal structure of mitoxin II, a manomeric Lys49-Phospholipase 'A IND. 2' homologue isolated from the venom of Cerrophidion (Bothrops) godmani
- Site-directed mutagenesis of the interface region of a Lys49 Phospholipase A2 Homodimeric Homologue: Bothropstoxin-I
Informações sobre o DOI: 10.1016/j.pep.2009.04.006 (Fonte: oaDOI API)
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