Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 Mar 21;114(14):E2826–E2835. doi: 10.1073/pnas.1613447114

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

PMC Copyright notice

Fig. 3. — IDE binds to phosphatidylinositol-containing liposomes and PtdIns(4,5)P2 activates the enzyme. (A) IDE binding to liposomes was tested using 260 μg of total lipid and 0.9 µg of IDE. Liposomes isolated after incubation were separated on a polyacrylamide gel and stained by Western blotting with anti-IDE antibody. Lane 1 (MW Std), molecular weight markers; lane 2 (empty well), no IDE or liposomes; lane 3 (PC), IDE plus liposomes containing only DOPC; lane 4 (PtdIns 4,5 diP), IDE plus DOPC liposomes with PtdIns(4,5)P2 at a ratio of 10:1; lane 5 (IDE alone), enzyme only; lane 6 (input), 0.1 µg of purified IDE without incubation. (B) Comparison of IDE activation by PtdIns(4,5)P2 (di-C16 or di-C8 acyl chains), Ins(4,5)P2, phosphatidylserine, and phosphatidylcholine. IDE activity was measured by the hydrolysis of Abz-GGFLRKHGQ-Eddnp substrate at varying concentrations of the indicated lipid or Ins(4,5)P2. The curves for activation by PtdIns(4,5)P2 (di-C8 acyl chains) and Ins(4,5)P2 are the fits to a hyperbolic function. Curves are drawn through the data points for activation by other compounds to show trends.