Measurement of Trace Elements in Proteins Extracted from Liver by Size Exclusion Chromatography-Inductively Coupled Plasma-Mass Spectrometry with a Magnetic Sector Mass Spectrometer
Autor: | Daniel R. Wiederin, Robert S. Houk, Jin Wang, Dawn Dreessen |
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Rok vydání: | 2001 |
Předmět: |
Size-exclusion chromatography
Biophysics Analytical chemistry chemistry.chemical_element Mass spectrometry Biochemistry Mass Spectrometry Sector mass spectrometer Magnetics Metalloprotein Animals Molecular Biology Inductively coupled plasma mass spectrometry Chromatography High Pressure Liquid chemistry.chemical_classification Cadmium Chromatography Chemistry Osmolar Concentration Polyatomic ion Proteins Cell Biology Hydrogen-Ion Concentration Small molecule Trace Elements Molecular Weight Liver Metals Calibration Chromatography Gel Cattle Metallothionein |
Zdroj: | Analytical Biochemistry. 288:89-96 |
ISSN: | 0003-2697 |
DOI: | 10.1006/abio.2000.4885 |
Popis: | Proteins are extracted from liver into aqueous buffer at pH 7 and separated by size exclusion chromatography (SEC). Inductively coupled plasma mass spectrometry (ICP-MS) with a magnetic sector mass spectrometer is used to identify those protein fractions that contain Cu, Zn, Mn, Fe, Cd, S, P, Mo, Co, Ca, or Mg. The experimental setup provides very high sensitivity. Measurements at medium spectral resolution remove polyatomic interferences for some difficult elements like Fe, S, and P. Some elements are found in different molecular weight proteins; for example, cadmium binds to four different protein fractions (>400 kDa, 70 kDa, and metallothionein). Other elements like Mo, Ca, and Mg are present only in low-molecular-weight proteins or other small molecules. |
Databáze: | OpenAIRE |
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