new approach to the depletion of albumin and immunoglobulin G from human serum

The use of proteomic analysis to find potential diagnostic biomarkers is limited by the presence of serum albumin (HSA) and immunoglobulin (IgG) at high concentrations in patients’ blood; these substances impede the detection of serum proteins with similar molecular weights. Recombinant HSA- and IgG...

Full description

Saved in:
Bibliographic Details
Published in:Applied biochemistry and microbiology 2015-05, Vol.51 (3), p.367-373
Main Authors: Bormotova, E. A, Mil’man, B. L, Gupalova, T. V
Format: Article
Language:English
Subjects:
adsorbents
affinity chromatography
antibodies
Biochemistry
Biomarkers
Biomedical and Life Sciences
blood serum
Body fluids
Chromatography
Diagnostics
humans
immunoglobulin G
Immunoglobulins
Life Sciences
Medical Microbiology
Microbiology
molecular weight
patients
polypeptides
Proteomics
serum albumin
Sorbents
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 use of proteomic analysis to find potential diagnostic biomarkers is limited by the presence of serum albumin (HSA) and immunoglobulin (IgG) at high concentrations in patients’ blood; these substances impede the detection of serum proteins with similar molecular weights. Recombinant HSA- and IgG-binding polypeptides are used as ligands in creating sorbents for complete removal of the proteins by affinity chromatography. The binding specificity of the sorbents for HSA and IgG is higher than that of the conventionally used antibodies. A composite sorbent enabling the depletion of HSA and IgG from serum by single-step affinity chromatography was obtained. The developed sorbents were used to prepare serum for proteomic analysis.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683815030047