Purification and characterization of receptors for myoinositol trisphosphate and myoinositol tetrakis phosphate from Entamoeba histolytica.
Indian J Biochem Biophys
;
2001 Aug; 38(4): 253-7
Artículo
en Inglés
| IMSEAR
| ID: sea-27133
ABSTRACT
The microsomal fraction from the log phase of Entamoeba histolytica cells contains Ins(1,4,5)P3 and Ins(1,3,4,5)P4 binding activity. The binding proteins/receptors for both Ins(1,4,5)P3 and Ins(1,3,4,5)P4 were purified and found to be specific for each ligand. The molecular masses for native proteins for InsP3 and InsP4 are 138 kDa and 130 kDa respectively having subunits of 69 kDa and 64 kDa respectively. That these proteins are associated with Ca2+ release was confirmed by including these proteins separately in proteoliposomes and adding InsP3 and InsP4 in both the cases.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Proteolípidos
/
Sitios de Unión
/
Canales de Calcio
/
Inositol 1,4,5-Trifosfato
/
Membrana Celular
/
Calcio
/
Receptores Citoplasmáticos y Nucleares
/
Subunidades de Proteína
/
Entamoeba histolytica
/
Receptores de Inositol 1,4,5-Trifosfato
Idioma:
Inglés
Revista:
Indian J Biochem Biophys
Año:
2001
Tipo del documento:
Artículo
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