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

Banabihari Giri, Ruma Das, Sanghamitra Raha, Susweta Biswas

Research output: Contribution to journalArticle

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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.

Original languageEnglish (US)
Pages (from-to)253-257
Number of pages5
JournalIndian Journal of Biochemistry and Biophysics
Volume38
Issue number4
StatePublished - Aug 1 2001
Externally publishedYes

Fingerprint

Entamoeba histolytica
Inositol
Purification
Phosphates
Proteins
Molecular mass
Carrier Proteins
Ligands
inositol-1,3,4,5-tetrakisphosphate

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

Cite this

Purification and characterization of receptors for myoinositol trisphosphate and myoinositol tetrakis phosphate from Entamoeba histolytica. / Giri, Banabihari; Das, Ruma; Raha, Sanghamitra; Biswas, Susweta.

In: Indian Journal of Biochemistry and Biophysics, Vol. 38, No. 4, 01.08.2001, p. 253-257.

Research output: Contribution to journalArticle

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