Stability of '('alfa''beta') IND. 2' form of Na, K-ATPase: conformational states in the presence of chemical agents and thermal denaturation (2004)
- Authors:
- USP affiliated authors: WARD, RICHARD JOHN - FFCLRP ; CIANCAGLINI, PIETRO - FFCLRP
- Unidade: FFCLRP
- Assunto: ENZIMAS (ESTRUTURA)
- Language: Inglês
- Imprenta:
- Publisher: Laboratório Nacional de Luz Sincroton - LNLS
- Publisher place: Campinas
- Date published: 2004
- Source:
- Título do periódico: Abstracts and Program
- Conference titles: Latin American Protein Society Meeting
-
ABNT
RIGOS, C. F. et al. Stability of '('alfa''beta') IND. 2' form of Na, K-ATPase: conformational states in the presence of chemical agents and thermal denaturation. 2004, Anais.. Campinas: Laboratório Nacional de Luz Sincroton - LNLS, 2004. . Acesso em: 23 abr. 2024. -
APA
Rigos, C. F., Santos, H. L., Ward, R. J., & Ciancaglini, P. (2004). Stability of '('alfa''beta') IND. 2' form of Na, K-ATPase: conformational states in the presence of chemical agents and thermal denaturation. In Abstracts and Program. Campinas: Laboratório Nacional de Luz Sincroton - LNLS. -
NLM
Rigos CF, Santos HL, Ward RJ, Ciancaglini P. Stability of '('alfa''beta') IND. 2' form of Na, K-ATPase: conformational states in the presence of chemical agents and thermal denaturation. Abstracts and Program. 2004 ;[citado 2024 abr. 23 ] -
Vancouver
Rigos CF, Santos HL, Ward RJ, Ciancaglini P. Stability of '('alfa''beta') IND. 2' form of Na, K-ATPase: conformational states in the presence of chemical agents and thermal denaturation. Abstracts and Program. 2004 ;[citado 2024 abr. 23 ] - Influence of enzyme conformational changes catalytic activity investigated by circular dichroism spectroscopy
- The study of the association of the ('alfa''beta) protomer of Na, K-ATPase solubilized with 'C IND.12''E IND. 8'
- Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE
- Thermal denaturation of the Na,K-ATPase solubilized and incorporated in DPPC:DPPE-liposomes
- Influence of enzyme conformational changes on catalytic activity of solubilized Na,K-ATPase investigated by circular dichroism spectroscopy
- pH effects in Na, K-ATPase: catalytic activity, fluorescence and circular dichroism analysis
- Estabilidade térmica da Na, K-ATPase solubilizada e incorporada em lipossomos de DPPC:DPPE
- The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity
- Circular dichroism associated with surface tension and dilatational elasticity to study the association of NA,K-ATPase subunits
- Crystal structure of mitoxin II, a manomeric Lys49-Phospholipase 'A IND. 2' homologue isolated from the venom of Cerrophidion (Bothrops) godmani
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