Characterization of the myoglobin peroxidase activity in the absence and in the presence of the proteolytic enzyme thimet-oligopeptidase (TOP) wild type with different gluthatiolation degress (2008)
- Authors:
- Autor USP: FERRO, EMER SUAVINHO - ICB
- Unidade: ICB
- Assunto: HISTOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Abstracts
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq)
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ABNT
FERREIRA, J. C. et al. Characterization of the myoglobin peroxidase activity in the absence and in the presence of the proteolytic enzyme thimet-oligopeptidase (TOP) wild type with different gluthatiolation degress. 2008, Anais.. São Paulo: SBBq, 2008. . Acesso em: 31 dez. 2025. -
APA
Ferreira, J. C., Castro, L. M., Ferro, E. S., Oliveira, V., Demasi, M., & Nantes, I. L. (2008). Characterization of the myoglobin peroxidase activity in the absence and in the presence of the proteolytic enzyme thimet-oligopeptidase (TOP) wild type with different gluthatiolation degress. In Abstracts. São Paulo: SBBq. -
NLM
Ferreira JC, Castro LM, Ferro ES, Oliveira V, Demasi M, Nantes IL. Characterization of the myoglobin peroxidase activity in the absence and in the presence of the proteolytic enzyme thimet-oligopeptidase (TOP) wild type with different gluthatiolation degress. Abstracts. 2008 ;[citado 2025 dez. 31 ] -
Vancouver
Ferreira JC, Castro LM, Ferro ES, Oliveira V, Demasi M, Nantes IL. Characterization of the myoglobin peroxidase activity in the absence and in the presence of the proteolytic enzyme thimet-oligopeptidase (TOP) wild type with different gluthatiolation degress. Abstracts. 2008 ;[citado 2025 dez. 31 ] - Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)
- Calcium-mediated membrane association of endopeptidase 24.15(EC3.4.24.15)
- 14-3-3 Epsilon modulates the stimulated secretion of endopeptidase 24.15
- 14.3.3 plays important role on endopeptidase 24.15 (EC 3.4.24.25) secretion
- Novos mecanismos de secreção e associação extracelular de proteínas: implicações no metabolismo celular de peptídeos
- Metalloendopeptidase EC 3.4.24.15 is targeted to and secreted from the regulated secretory pathway in AtT-20 cells
- Imuno-histoquímica para microscopia eletrônica revela a distribuição subcelular da EC 3.4.24.15 no cérebro de ratos
- Identificação de proteína que se ligam a thimet-oligopeptidase (E.C.3.4.24.15) no sistema nervoso central, utilizando two hybrid system
- Hypotensive action of hemopressin, an endogenous peptide substrate of metalloendopeptidase 24.15
- Confocal microscopy reveals thimet oligopeptidase (EC 3.4.24.15) and neurolysin (EC 3.4.24.16) in the classical secretory pathway
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