Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability.
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Smith SD, She YM, Roberts EA, Sarkar B
Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability.
J Proteome Res. 2004 Jul-Aug;3(4):834-40.
- PubMed ID
- 15359738 [ View in PubMed]
- Abstract
To further our knowledge of intracellular copper transport, we used a proteomics strategy to search for hepatic proteins with copper-binding ability. Hep G2 cytosolic and microsomal fractions were applied to a copper(II)-loaded immobilized metal-affinity chromatography (IMAC) column. Protein identification was performed with 2-D gel electrophoresis and mass spectrometry. We identified 48 cytosolic proteins and 19 microsomal proteins displaying copper-binding ability. These proteins are diverse in function. Fifty-two of the 67 proteins contain putative metal-binding domains. We have identified many components of the Hep G2 copper metalloproteome including a large number of proteins not previously known to bind copper.
DrugBank Data that Cites this Article
- Drug Targets
- Drug Carriers
Drug Carrier Kind Organism Pharmacological Action Actions Copper Serum albumin Protein Humans NoBinderDetails