Purification and characterization of receptors for myoinositol trisphosphate and myoinositol tetrakis phosphate from Entamoeba histolytica

Authors
Giri, B Das, R Raha, S Biswas, S
Citation
B. Giri et al., Purification and characterization of receptors for myoinositol trisphosphate and myoinositol tetrakis phosphate from Entamoeba histolytica, I J BIOCH B, 38(4), 2001, pp. 253-257
Citations number
18
Categorie Soggetti
Biochemistry & Biophysics
Journal title
INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS
ISSN journal
03011208 → ACNP
Volume
38
Issue
4
Year of publication
2001
Pages
253 - 257
Database
ISI
SICI code
0301-1208(200108)38:4<253:PACORF>2.0.ZU;2-I
Abstract
The microsomal fraction from the log phase of Entamoeba histolytica cells c ontains Ins(1,4,5)P-3 and Ins(1,3,4,5)P-4 binding activity. The binding pro teins/receptors for both Ins(1,4,5)P-3 and Ins(1,3,4,5)P-4 were purified an d found to be specific for each ligand. The molecular masses for native pro teins for InsP(3) and InsP(4) are 138 kDa and 130 kDa respectively having s ubunits of 69 kDa and 64 kDa respectively. That these proteins are associat ed with Ca2+ release was confirmed by including these proteins separately i n proteoliposomes and adding InsP(3) and InsP(4) in both the cases.