Please use this identifier to cite or link to this item:
Title: Identification of proteins related to nickel homeostasis in Helicobater pylori by immobilized metal affinity chromatography and two-dimensional gel electrophoresis
Authors: Sun, X;Ge, R;Chiu, JF;Sun, H;He, QY
subject: Chemistry;Analytical chemistry pharmacy and pharmacology
Year: 2008
Publisher: Hindawi Publishing Corp. The Journal's web site is located at
Description: Helicobacter pylori (H. pylori) is a widespread human pathogen causing peptic ulcers and chronic gastritis. Maintaining nickel homeostasis is crucial for the establishment of H. pylori infection in humans. We used immobilized-nickel affinity chromatography to isolate Ni-related proteins from H. pylori cell extracts. Two-dimensional gel electrophoresis and mass spectrometry were employed to separate and identify twenty two Ni-interacting proteins in H. pylori. These Ni-interacting proteins can be classified into several general functional categories, including cellular processes (HspA, HspB, TsaA, and NapA), enzymes (Urease, Fumarase, GuaB, Cad, PPase, and DmpI), membrane-associated proteins (OM jhp1427 and HpaA), iron storage protein (Pfr), and hypothetical proteins (HP0271, HP jhp0216, HP jhp0301, HP0721, HP0614, and HP jhp0118). The implication of these proteins in nickel homeostasis is discussed.
URI: Article ID 289490&spage=&epage=&date=2008&atitle=Identification+of+proteins+related+to+nickel+homeostasis+in+Helicobater+pylori+by+immobilized+metal+affinity+chromatography+and+two-dimensional+gel+electrophoresis
Standard no: Metal-Based Drugs, 2008, v. 2008 Article ID 289490
Appears in Collections:Department of Anatomy

Files in This Item:
Click on the URI links for accessing contents.

Items in HannanDL are protected by copyright, with all rights reserved, unless otherwise indicated.