| Literature DB >> 7811237 |
M Hirata1, T Kanematsu, K Sakuma, T Koga, Y Watanabe, S Ozaki, H Yagisawa.
Abstract
D-myo-Inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) binding domain of phospholipase C-delta 1 (PLC-delta 1) was determined by examining binding activity of the synthetic peptide corresponding to residues 30-43 of PLC-delta 1. The peptide coupled with carrier proteins such as keyhole limpet hemocyanin or bovine serum albumin bound Ins(1,4,5)P3, whereas a scrambled peptide with the same amino acids did not do so. Polyclonal antibody against the peptide was examined to determine whether it would cause inhibition of the Ins(1,4,5)P3 binding to PLC-delta 1. Fab fragment of antibody to the peptide did inhibit binding to PLC-delta 1, in a dose-dependent manner. Thus it seems likely that the region of residues 30-43 of PLC-delta 1 is responsible for the binding of Ins(1,4,5)P3.Entities:
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Year: 1994 PMID: 7811237 DOI: 10.1006/bbrc.1994.2845
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575