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
Artigo
em Inglês
| 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:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Proteolipídeos
/
Sítios de Ligação
/
Canais de Cálcio
/
Inositol 1,4,5-Trifosfato
/
Membrana Celular
/
Cálcio
/
Receptores Citoplasmáticos e Nucleares
/
Subunidades Proteicas
/
Entamoeba histolytica
/
Receptores de Inositol 1,4,5-Trifosfato
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
2001
Tipo de documento:
Artigo
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