By Harold M. McNair, James M. Miller
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The advantage of proteinA–proteinG affinity approaches is that they are applicable to various species, which is not the case for immunoadsorption. In spite of their pretty good specificity, protein A and protein G used alone are not capable of removing all immunoglobulin G subclasses. Positioning protein G as a firstaffinity depletion followed by the protein A column is probably the best combination for removing most of these immunoglobulins. , 2007), with the advantage of a larger specificity and coverage toward antibody classes.
Paper Symposium: Two dimensional gel protein databases. Electrophoresis. 1994b;15:1347–1492. ). Paper Symposium: Two dimensional gel Protein databases. Electrophoresis. 1995;16:2175–2264. ). Paper Symposium: Two dimensional gel protein databases. Electrophoresis. 1996;17:1653–1798. ). Genomics and proteomics of cancer. Electrophoresis. 1999;20:223–428. Chenau J, Michelland S, Sidibe J, Seve M. Peptides OFFGEL electrophoresis: A suitable pre-analytical step for complex eukaryotic samples fractionation compatible with quantitative iTRAQ labeling.
This is an important issue because, after having removed the abundant species present, all other proteins will remain dilute (and even more dilute than in the initial sample), with almost no possibility of getting concentrated, whatever the means, without a large risk of losing many species. The removal of high-abundance proteins also has an impact on the reduction of the dynamic concentration range whose extent depends on the capability of specifically targeting the most representative proteins.
Basic gas chromatography by Harold M. McNair, James M. Miller