Separation of antithrombin III variants by micellar electrokinetic chromatography

The characterisation of proteins is still one of the most challenging analytical tasks in modern bioanalysis. Due to the complex structure of proteins, several analytical techniques are often required to get sufficient information. Antithrombin III (AT III), a high-molecular-mass plasma glycoprotein...

Full description

Saved in:
Bibliographic Details
Published in:Journal of Chromatography A 2001-07, Vol.924 (1), p.307-313
Main Authors: Dönges, Reiner, Römisch, Jürgen, Stauss, Harald, Brazel, Dieter
Format: Article
Language:English
Subjects:
Analysis
Antithrombin III - isolation & purification
Antithrombin III - metabolism
Antithrombins
Biological and medical sciences
Chromatography, Micellar Electrokinetic Capillary - methods
Enzyme inhibitors
General pharmacology
Glycoprotein
Heparin
Heparin - metabolism
Humans
Investigative techniques, diagnostic techniques (general aspects)
Medical sciences
Miscellaneous. Technology
Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques
Pharmacology. Drug treatments
Proteins
Sample injection
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The characterisation of proteins is still one of the most challenging analytical tasks in modern bioanalysis. Due to the complex structure of proteins, several analytical techniques are often required to get sufficient information. Antithrombin III (AT III), a high-molecular-mass plasma glycoprotein which is an important protease inhibitor and the main modulator of thrombin activity, circulates in plasma in two isoforms, the so-called AT III-α (90–95%) and -β (5–10%). Micellar electrokinetic chromatography was used to analytically separate these AT III variants, which differ in their affinity to the polysaccharide heparin.
ISSN:0021-9673
DOI:10.1016/S0021-9673(01)00827-5