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Topic: Affinity chromatography

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	* Affinity chromatography - (Biology): Definition
		Affinity chromatography is a method of separating biochemical mixtures, based on a highly specific biologic interaction such as that between antigen and antibody, enzyme and substrate, or receptor and ligand.
		Affinity chromatography is a biochemical separation method that combines size fractionation capability of gel permeation chromatography with the ability to design a stationary phase that reversibly binds to a known subset of molecules.
		Used in affinity chromatography to purify glycoproteins and as reagents for detecting glycoproteins.
	en.mimi.hu /biology/affinity_chromatography.html (156 words)

	Antibody Purification Affinity Chromatography
		Affinity chromatography can also be used to purify antigens from complex mixtures by using beads coated with specific antibody.
		Affinity chromatography uses antigen-antibody binding to purify antigens or antibodies.
		To purify a specific antigen from a complex mixture of molecules, a monoclonal antibody is attached to an insoluble matrix, such as chromatography beads, and the mixture of molecules is passed over the matrix.
	www.antibodystation.com /antibody-affinity-chromatography (227 words)

	Genotech - Affinity chromatography and resins
		Affinity Chromatography Resins: for the separation and purification of affinity tagged proteins and for the binding of immunoglobulin molecules.
		The advances in affinity chromatography have enabled researchers to purify large quantities of highly pure proteins for a multitude of analysis techniques, including crystallography, protein:protein studies and in-vitro assays.
		Affinity chromatography works by binding a protein, via a reversible interaction, to a specific ligand that is prebound to a solid chromatographic support.
	www.gbiosciences.com /affinity-products.aspx (562 words)

	3
		The general philosophy of affinity chromatography is that for a specific protein there are ligands that interact with that protein reversibly and which, if immobilized on a support material, specifically retard the chromatography of that protein and allow its purification.
		Except in the case of covalent affinity chromatography, the interaction of the protein with the matrix ligand is reversible, and it is this interaction that retards the passage of the specifically adsorbed protein.
		Affinity techniques are almost always used with some form of prior fractionation, usually because the sheer amount of protein obtained in initial homogenization or extraction is too large to employ the generally small bed volumes of affinity resins.
	www.richmond.edu /~jbell2/CHAPT3.html (4856 words)

	Affinity chromatography
		Affinity chromatography can be performed using a number of different protein tags.
		An interaction is detected as depletion of the labeled protein from the flow-through and presence of the protein in the experimental column eluate.
		Affinity chromatography with FTZ (1st 3 lanes) and control (2nd 3 lanes) affinity columns.
	www.utoronto.ca /krause/affinity.html (948 words)

	Affinity chromatography
		In general, affinity chromatography achieves a higher purification factor (with a median value in reported purifications of about ten fold) than ion-exchange chromatography (with a median performance of about three fold), in spite of it generally being used at a later stage in the purification when there is less purification possible.
		This dye-affinity chromatography was allegedly discovered by accident, certain enzymes being found to bind to the blue-dyed dextran used, as a molecular weight standard, to calibrate gel exclusion columns.
		Affinity chromatography is not used extensively in the large-scale manufacture of enzymes, primarily because of cost.
	www.lsbu.ac.uk /biology/enztech/affinity.html (548 words)

	Affinity Chromatography by Jennifer Henry (Site not responding. Last check: 2007-10-29)
		Affinity chromatography is a technique which allows for the separation of specific molecules, mostly proteins, from a solution, in which there are many different proteins.
		A specific example in which affinity chromatography is used is when a solution of impure insulin receptors is passed through a column containing the insulin protein.
		The affinity chromatography technique shows the interactions between different molecules, as well as providing a means to separate molecules from a mixture.
	www.samford.edu /~gekeller/henry.html (304 words)

	Affinity Chromatography
		Affinity Chromatography is based on the principle of biological recognition.
		The first step in affinity chromatography is to prepare a stationary phase by immobilizing one of the two recognized components on an insoluble hydrophobic polymer such as agarose.
		There are thousands of examples of affinity chromatography in the literature, including the purification of trypsin and other serine proteases using immobilized bovine pancreatic trypsin inhibitor as the stationary phase.
	www.rit.edu /~pac8612/webionex/website/html/ione08ah.html (205 words)

	TCAW 9/98: Creating A Central Science
		As with all forms of chromatography, the choice of coating, whether inert or reactive, depends on the nature of the material to be separated and the end results desired.
		Affinity chromatography, developed in the 1930s, was first used to study enzymes and other proteins.
		Chromatography - with its fundamental quest to separate and identify every kind of atom and molecule, and with its diverse applications from agriculture to zoology, from petrochemicals to biopharmaceuticals, and from simple salts to the most complex polymers - can indeed be considered the instrumental backbone of chemistry's claim to be the central science.
	pubs.acs.org /hotartcl/tcaw/98/sep/creat.html (2058 words)

	affinity chromatography (Site not responding. Last check: 2007-10-29)
		The affinity material is made from a solid support like Sephadex or Sepharose gel to which a spacer group may be added and then the inhibitor (resembling the enzyme's substrate) is covalently bound.
		Affinity material is put in a column and an extract containing a mixture of proteins is applied to the column
		Free substrate (inhibitor) will bind more tightly to the bound inhibitor on the affinity material since free substrate (inhiibitor) can be applied at a high concentration and the enzyme has a higher affinity for free substrate as compared to bound substrate/inhiibitor.
	www.bio.mtu.edu /campbell/482w91a.htm (204 words)

	GE Healthcare Life Sciences - Affinity Chromatography
		Affinity chromatography (AC) is a technique enabling purification of a biomolecule with respect to biological function or individual chemical structure.
		The substance to be purified is specifically and reversibly adsorbed to a ligand (binding substance), immobilized by a covalent bond to a chromatographic bed material (matrix).
		Affinity chromatography media are commonly used for applications such as purification of fusion proteins, mono- and polyclonal antibodies, and glycoproteins.
	www4.amershambiosciences.com /aptrix/upp00919.nsf/Content/LabSep_EduC~LC_tech~AC (204 words)

	The Biotechnology Project: Ion Exchange Chromatography
		The term “chromatography” applies to a wide range of separation techniques that are based on the differential interaction of molecules between a moving phase and a stationary phase.
		Affinity chromatography separates based on biological affinity for specific molecules, such as antigen-antibody interaction, metal binding capability, hormone receptor interactions, etc. Although the focus of this chapter is on ion exchange chromatography since that is used in the current purification, other types of chromatography will be discussed in lecture.
		Chromatography is often performed using instrumentation including a pump to force liquid through the column, a UV detector with chart recorder to automatically measure and record the absorbance at 280, and a fraction collector to automatically move the tubes after a volume of liquid has been collected.
	matcmadison.edu /biotech/resources/proteins/labManual/chapter_4/section4_4.htm (3431 words)

	The Scientist : Liquid Chromatography: Products in the Protein Chemist's Tool Chest
		Modern liquid chromatography has come a long way since its infancy-when early matrices were capable of providing only crude separations-to modern matrices and technologies that can accomplish the purification of a protein to homogeneity in a single chromatographic step.
		Ion exchange chromatography (IEC) is based upon the net charge of a protein at a given pH and the charge-dependent affinity between the protein and charges on a support matrix.
		Affinity chromatography has progressed immensely from its inception, when insoluble materials such as starch, cellulose, and phosphocellulose were the only matrices available.
	www.the-scientist.com /article/display/17960 (1853 words)

	IMAC (Site not responding. Last check: 2007-10-29)
		Affinity enrichment of phosphoproteins serves to eliminate interferences and to increase signal in protein identification experiments, which is particularly important in the case of polypeptides phosphorylated at multiple sites because they exhibit signal suppression in sequencing experiments using positive-ion electrospray ionization MS-MS.
		Photolabeled peptides were isolated by a new procedure that used metal chelate chromatography to affinity purify the photolabeled peptides prior to final purification by reverse-phase HPLC.
		Aluminum(III)-chelate or iron(III)-chelate affinity chromatography and reversed-phase HPLC were used to purify photolabel-containing peptides generated with either trypsin or chymotrypsin.
	www.altcorp.com /affinitylabeling/imac.htm (1460 words)

	GE Healthcare Life Sciences - Affinity Chromatography
		Affinity chromatography (AC) is a technique enabling purification of a biomolecule with respect to biological function or individual chemical structure.
		The substance to be purified is specifically and reversibly adsorbed to a ligand (binding substance), immobilized by a covalent bond to a chromatographic bed material (matrix).
		Affinity chromatography media are commonly used for applications such as purification of fusion proteins, mono- and polyclonal antibodies, and glycoproteins.
	www6.gelifesciences.com /aptrix/upp00919.nsf/Content/LabSep_EduC~LC_tech~AC (204 words)

	Affinity Chromatography — from Textile Dyes to Synthetic Ligands by Design, Part I - BioPharm International
		At its widest definition, affinity chromatography encompasses techniques from immobilized metal chelate affinity to molecular imprinting and technologies from affinity capillary electrophoresis to affinity precipitation, affinity partitioning, and affinity membranes.
		The advent of affinity chromatography is usually attributed to Cuatrecasas, Wilchek, and Anfinsen.
		This paper identified an initial problem with dye affinity chromatography, namely the leakage of the dye into the eluate (properties of synthetic adsorbents will be discussed next month in Part II of this article).
	www.biopharminternational.com /biopharm/article/articleDetail.jsp?id=104326 (850 words)

	The Christian B. Anfinsen Papers: Molecular Engineering and Affinity Chromatography, 1959-1972
		Anfinsen believed that the mystique surrounding deoxyribonucleic acid (DNA), the structure of which was described by Francis H. Crick and James D. Watson, was overshadowing the field of protein chemistry.
		By 1966, Anfinsen and his colleagues had isolated the Staphylococcus aureus RNase through the use of affinity chromatography, an innovative laboratory technique first developed in 1951 by Dan Hampston Campbell, a professor of immunology at the California Institute of Technology.
		Affinity chromatography enabled Anfinsen to put a bacterium into a chemical solution that selectively captures molecular particles and spreads them out across a medium so that they can be easily examined, in analogy to the colors of a spectrum.
	profiles.nlm.nih.gov /KK/Views/Exhibit/narrative/molecular.html (590 words)

	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 blood serum.
		For example, the antibodies in a serum sample specific for a particular antigenic determinant can be isolated by the use of affinity chromatography.
		Link to a discussion of another chromatographic technique: exclusion chromatography.
	users.rcn.com /jkimball.ma.ultranet/BiologyPages/A/AffinityChrom.html (250 words)

	The Scientist : Tag! Purifying Proteins with Affinity Chromatography
		In gel filtration chromatography (middle), proteins are resolved by size, using porous beads that selectively slow the migration of appropriately sized molecules.
		While IMAC and other affinity tag systems are ideal for a fast, effective first step, most scientists caution that they often must be followed by a second chromatographic step to remove salts and other contaminants.
		Additionally, since the two affinity tags do not need to be present on the same protein, the method can be used to copurify interacting proteins that contain one or the other tag.
	www.the-scientist.com /article/display/15284 (1530 words)

	Biotech Bunny: Affinity Chromatography
		Affinity chromatography involves the use of packing which has been chemically modified by attaching a compound with a specific affinity for the desired molecules, primarily biological compounds.
		The ligands, or "affinity tails", that are inserted into the matrix can be genetically engineered to possess a specific affinity.
		In a process similar to ion exchange chromatography, the desired molecules adsorb to the ligands on the matrix until a solution of high salt concentration is passed through the column.
	www.rpi.edu /dept/chem-eng/Biotech-Environ/CHROMO/chromaffinity.html (157 words)

	NSDL Metadata Record -- Affinity Chromatography
		This is an experiment showing the application of affinity chromatography to the separation of albumin from horse serum.
		A brief introduction of affinity chromatography and how it is being used in this specific experiment is given.
		This appears to be a good experiment to show the advantages of affinity chromatography in separating specific proteins from a complex matrix and would be useful in a biochemistry course or a course that is specifically looking at differing types of chromatography.
	nsdl.org /mr/334086 (78 words)

	Chromatography
		Column chromatography is one of the most common methods of protein purification.
		Where ion exchange chromatography relies on the charges of proteins to isolate them, hydrophobic interaction chromatography uses the hydrophobic properties of some proteins.
		Affinity chromatography relies on the biological functions of a protein to bind it to a column.
	lifesciences.asu.edu /resources/mamajis/chromatography/chromatography.html (1005 words)

	Affinity Chromatography
		Affinity chromatography is the purification of a biomolecule with respect to the specific binding of that biomolecule due to its chemical structure (Amersham Bioscience, 2003).
		In recent years some of the most exciting applications for affinity chromatography have arisen, particularly in the area of recombinant DNA technology.
		Still, the main area of concentration for affinity chromatography applications continues to be in protein purification (Parikh, 1993).
	www.bio.davidson.edu /Courses/Molbio/MolStudents/spring2003/WoodW/affchrom1.html (445 words)

	C42 Affinity Chromatography (Site not responding. Last check: 2007-10-29)
		Affinity chromatography takes advantage of the strong binding interaction which an antigen and an antibody have for one another by incorporating one of them into the stationary phase of a chromatographic resin.
		The antigen may be separated from a mixture as a result of this strong affinity and high degree of specificity.
		A portion of the affinity resin is prepared by attaching monoclonal antibody.
	chemmovies.unl.edu /Chemistry/biotech/C42c.html (474 words)

	Affinity Chromatography, etc. spring 2002 (Site not responding. Last check: 2007-10-29)
		This refers to the use as adsorbents in chromatography of materials with groups which are supposed to be specific ligands of the protein being purified.
		Many materials for affinity chromatography are commercially available, complete (if they bind many proteins or a very important one - for example 5'-AMP-agarose), with spacer arms, or just activated.
		Elution from affinity columns may be with the free ligand in solution, which competes with the bound ligand for the protein's binding site; or may be a non-specific method such as high salt.
	aesop.rutgers.edu /~dbm/affinity.html (2622 words)

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