Molecular Separation /
Background Information: A major goal in the
biochemistry or molecular biology laboratory is the isolation of a specific protein from complex mixtures. Such isolation procedures
often involve several fractionation steps with the effectiveness of each step monitored by electrophoresis. Chromatography is a type
of fractionation similar to electrophoresis in that proteins separate from each other as they are passed through a matrix. With chromatography,
however, solvent flow (by gravity, pressure or capillary action), not an electric field, carries the proteins through the matrix.
The separation occurs because proteins interact with various matrices in different ways. Chromatography matrices are designed to exploit
the physical and chemical interactions of a protein of interest. For example, acidic proteins will interact with a basic matrix to
a greater extent than basic or neutral proteins so a basic matrix can be used to separate acidic proteins (which will interact with
the matrix and be retained) from non-acidic proteins (which will flow through the matrix). The acidic proteins retained by the matrix
can then be removed or eluted by disrupting their interactions with the matrix. The major limitation of most types of chromatography
is the lack of specificity for only one protein, for example a basic matrix willretain all acidic proteins to various extents and
not just the specific protein of interest. ¡
Affinity Chromatography ¨C A Handbook
Affinity chromatography separates proteins
on the basis of a reversible interaction ... This handbook describes the role of affinity chromatography in the ...
fachschaft.biochemtech.uni-halle.de/downloads/chromatography/affchr.pdf
Affinity
chromatography - Wikipedia, the free encyclopedia
Affinity chromatography is a chromatographic method of separating biochemical mixtures,
based on a highly specific biologic interaction such as that between ...
en.wikipedia.org/wiki/Affinity_chromatography
The goal of affinity chromatography is to separate all the molecules of a particular specificity from the whole gamut
of molecules in a mixture such as a ...
users.rcn.com/jkimball.ma.ultranet/BiologyPages/A/AffinityChrom.html
Restek
¡¤ From the Beginning ¡¤ Phases ¡¤ Phase creation ¡¤ Conducting an analysis ...
ull.chemistry.uakron.edu/chemsep/affinity/
Affinity
Chromatography Method
Affinity Chromatography Method. Affinity chromatography is designed to purify a particular protein from a mixed
sample. Figure 1. Loading affinity column. ...
www.bio.davidson.edu/Courses/genomics/method/Affinity.html
GE Healthcare Life
Sciences - Animation of affinity chromatography
If you have problem viewing affinity chromatography animation in the pop-up window,
... Download the Affinity chromatography animation below GE_Affinity.swf ...
www4.gelifesciences.com/aptrix/upp00919.nsf/Content/AD018C9E293F99BEC1256E92003E865A?OpenDocument
Affinity Chromatography - Sigma
Affinity chromatography is the process of bioselective adsorption and subsequent recovery of
a compound from an immobilized ligand.
www.sigmaaldrich.com/.../Protein_Analysis/Chromatography/Affinity_Chromatography.html
Protein A Mimetic (PAM) Affinity Chromatography: Immunoglobulins Purification ... Dye-Ligand Affinity Chromatography
for Protein Separation and Purification ...
www.springerprotocols.com/BookToc/doi/10.1007/978-1-60327-261-2
Affinity chromatography
system for parallel purification of ...
We describe the development and some application results of a simple affinity chromatography
system that can be used for the parallel purification of 24 ...
peds.oxfordjournals.org/cgi/content/full/15/10/775
Troubleshooting
affinity chromatography
Troubleshooting affinity chromatography. Problem: Tagged protein appears in washes, does not bind to affinity
resin. Possible cause ...
www.roche-applied-science.com/PROD_INF/MANUALS/epitope/p57-59.pdf
Web Guider
Ch 8.Immunohistoch / immunology
Ch 10.GC/MS, NMR and Proteomics