Identification and characterization of endonuclein binding proteins: evidence of modulatory effects on signal transduction and chaperone activity.

ABSTRACT:

Background

We have previously identified endonuclein as a cell cycle regulated WD-repeat protein that is up-regulated in adenocarcinoma of the pancreas. Now, we aim to investigate its biomedical functions.

Results

Using the cDNA encoding human endonuclein, we have expressed and purified the recombinant protein from Escherichia coli using metal affinity chromatography. The recombinant protein was immobilized to a column and by affinity chromatography several interacting proteins were purified from several litres of placenta tissue extract. After chromatography the eluted proteins were further separated by two-dimensional gel electrophoresis and identified by tandem mass spectrometry. The interacting proteins were identified as; Tax interaction protein 1 (TIP-1), Aalpha fibrin

SUBMITTER: Ludvigsen M 

PROVIDER: S-EPMC2810291 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature