299:
2474:
549:, is used. GST has an affinity for glutathione which is commercially available immobilized as glutathione agarose. During elution, excess glutathione is used to displace the tagged protein. CL7 has an affinity and specificity for Immunity Protein 7 (Im7) which is commercially available immobilized as Im7 agarose resin. For elution, an active and site-specific protease is applied to the Im7 resin to release the tag-free protein.
2254:
398:
of that antigen. This is also known as
Immunoaffinity Chromatography. For example, if an organism is immunised against a GST-fusion protein it will produce antibodies against the fusion-protein, and possibly antibodies against the GST tag as well. The protein can then be covalently coupled to a solid support such as agarose and used as an affinity ligand in purifications of antibody from immune serum.
586:
affinity matrix. p-aminobenyl-1-thio-β-D-galactopyranosyl agarose is used as the affinity matrix because it contains a galactopyranosyl group, which serves as a good substrate analog for E. coli β-Galactosidase. This property allows the enzyme to bind to the stationary phase of the affinity matrix and β-Galactosidase is eluted by adding increasing concentrations of salt to the column.
342:(PCC). The resin costs per amount of produced product can thus be drastically reduced. Since one column can always be eluted and regenerated while the other column is loaded, already two columns are sufficient to make full use of the advantages. Additional columns can give additional flexibility for elution and regeneration times, at the cost of additional equipment and resin costs.
482:
114:
biomolecules by disrupting their weaker interactions with the stationary phase, while the biomolecules of interest will remain bound. Target biomolecules may then be removed by applying a so-called elution buffer, which disrupts interactions between the bound target biomolecules and the ligand. The target molecule is thus recovered in the eluting solution.
315:
are usually done at ambient pressure. Alternatively, binding may be achieved using a batch treatment, for example, by adding the initial mixture to the solid phase in a vessel, mixing, separating the solid phase, removing the liquid phase, washing, re-centrifuging, adding the elution buffer, re-centrifuging and removing the elute.
307:
653:
based on their different weak affinities to an immobilized target. The higher affinity a compound has towards the target, the longer it remains in the separation unit, and this will be expressed as a longer retention time. The affinity measure and ranking of affinity can be achieved by processing the
397:
Another use for the procedure is the affinity purification of antibodies from blood serum. If the serum is known to contain antibodies against a specific antigen (for example if the serum comes from an organism immunized against the antigen concerned) then it can be used for the affinity purification
326:
A third method, expanded bed absorption, which combines the advantages of the two methods mentioned above, has also been developed. The solid phase particles are placed in a column where liquid phase is pumped in from the bottom and exits at the top. The gravity of the particles ensure that the solid
314:
Binding to the solid phase may be achieved by column chromatography whereby the solid medium is packed onto a column, the initial mixture run through the column to allow settling, a wash buffer run through the column and the elution buffer subsequently applied to the column and collected. These steps
585:
Another use for affinity chromatography is the purification of specific proteins using a gel matrix that is unique to a specific protein. For example, the purification of E. coli β-galactosidase is accomplished by affinity chromatography using p-aminobenyl-1-thio-β-D-galactopyranosyl agarose as the
337:
More recently, setups employing more than one column in series have been developed. The advantage compared to single column setups is that the resin material can be fully loaded since non-binding product is directly passed on to a consecutive column with fresh column material. These chromatographic
117:
Affinity chromatography does not require the molecular weight, charge, hydrophobicity, or other physical properties of the analyte of interest to be known, although knowledge of its binding properties is useful in the design of a separation protocol. Types of binding interactions commonly exploited
456:
Immunoaffinity chromatography is also the basis for immunochromatographic test (ICT) strips, which provide a rapid means of diagnosis in patient care. Using ICT, a technician can make a determination at a patient's bedside, without the need for a laboratory. ICT detection is highly specific to the
382:
Immunoaffinity media (detailed below) utilizes antigens' and antibodies' high specificity to separate; immobilized metal affinity chromatography is detailed further below and uses interactions between metal ions and proteins (usually specially tagged) to separate; nucleotide/coenzyme that works to
353:
By using affinity chromatography, one can separate proteins that bind to a certain fragment from proteins that do not bind that specific fragment. Because this technique of purification relies on the biological properties of the protein needed, it is a useful technique and proteins can be purified
465:
Immobilized metal ion affinity chromatography (IMAC) is based on the specific coordinate covalent bond of amino acids, particularly histidine, to metals. This technique works by allowing proteins with an affinity for metal ions to be retained in a column containing immobilized metal ions, such as
410:
or phosphate buffer, to neutralize the low pH elution buffer and halt any degradation of the antibody's activity. This is a nice example as affinity purification is used to purify the initial GST-fusion protein, to remove the undesirable anti-GST antibodies from the serum and to purify the target
401:
For thoroughness, the GST protein and the GST-fusion protein can each be coupled separately. The serum is initially allowed to bind to the GST affinity matrix. This will remove antibodies against the GST part of the fusion protein. The serum is then separated from the solid support and allowed to
113:
with which the ligand can react, forming stable covalent bonds. The stationary phase is first loaded into a column to which the mobile phase is introduced. Molecules that bind to the ligand will remain associated with the stationary phase. A wash buffer is then applied to remove non-target
375:
is nonspecific but mimics biological substrates and proteins. Glutathione is useful for separation of GST tagged recombinant proteins. Heparin is a generalized affinity ligand, and it is most useful for separation of plasma coagulation proteins, along with nucleic acid enzymes and lipases
626:-macroglobulin contamination, when performing mass spectrometry. In affinity purification of serum albumin, the stationary used for collecting or attracting serum proteins can be Cibacron Blue-Sepharose. Then the serum proteins can be eluted from the adsorbent with a buffer containing
568:
are proteins which can bind specific alpha-D-mannose and alpha-D-glucose carbohydrate molecules. Some common carbohydrate molecules that is used in lectin affinity chromatography are Con A-Sepharose and WGA-agarose. Another example of a lectin is wheat germ agglutinin which binds
452:
Immunoaffinity chromatography with monoclonal antibodies immobilized on monolithic column has been successfully used to capture extracellular vesicles (e.g., exosomes and exomeres) from human blood plasma by targeting tetraspanins and integrins found on the surface of the EVs.
429:
functional group which allows the peptide to be easily conjugated to a carrier protein (e.g. Keyhole limpet hemocyanin (KLH)). The same cysteine-containing peptide is also immobilized onto an agarose resin through the cysteine residue and is then used to purify the antibody.
714:
Aizpurua-Olaizola, Oier; Sastre Torano, Javier; Pukin, Aliaksei; Fu, Ou; Boons, Geert Jan; de Jong, Gerhardus J.; Pieters, Roland J. (January 2018). "Affinity capillary electrophoresis for the assessment of binding affinity of carbohydrate-based cholera toxin inhibitors".
597:
from E. coli can be purified using a DEAE-Cellulose matrix. A. phosphatase has a slight negative charge, allowing it to weakly bind to the positively charged amine groups in the matrix. The enzyme can then be eluted out by adding buffer with higher salt concentrations.
1841:
Meiby, E.; Simmonite, H.; Le Strat, L.; Davis, B.; Matassova, N.; Moore, J. D.; Mrosek, M.; Murray, J.; Hubbard, R. E.; Ohlson, S. (2013). "Fragment
Screening by Weak Affinity Chromatography: Comparison with Established Techniques for Screening against HSP90".
466:
cobalt, nickel, or copper for the purification of histidine-containing proteins or peptides, iron, zinc or gallium for the purification of phosphorylated proteins or peptides. Many naturally occurring proteins do not have an affinity for metal ions, therefore
1213:
Multia E, Tear CJ, Palviainen M, et al. (December 2019). "Fast isolation of highly specific population of platelet-derived extracellular vesicles from blood plasma by affinity monolithic column, immobilized with anti-human CD61 antibody".
322:
The ligands used in affinity chromatography are obtained from both organic and inorganic sources. Examples of biological sources are serum proteins, lectins and antibodies. Inorganic sources are moronic acid, metal chelates and triazine dyes.
1130:
Thompson, Nancy E.; Foley, Katherine M.; Stalder, Elizabeth S.; Burgess, Richard R. (2009). "Chapter 28 Identification, Production, and Use of Polyol-Responsive
Monoclonal Antibodies for Immunoaffinity Chromatography".
362:
Many different affinity media exist for a variety of possible uses. Briefly, they are (generalized) activated/functionalized that work as a functional spacer, support matrix, and eliminates handling of toxic reagents.
366:
Amino acid media is used with a variety of serum proteins, proteins, peptides, and enzymes, as well as rRNA and dsDNA. Avidin biotin media is used in the purification process of biotin/avidin and their derivatives.
318:
Sometimes a hybrid method is employed such that the binding is done by the batch method, but the solid phase with the target molecule bound is packed onto a column and washing and elution are done on the column.
544:
ions which have been immobilized by forming coordinate covalent bonds with a chelator incorporated in the stationary phase. For elution, an excess amount of a compound able to act as a metal ion ligand, such as
402:
bind to the GST-fusion protein matrix. This allows any antibodies that recognize the antigen to be captured on the solid support. Elution of the antibodies of interest is most often achieved using a low
370:
Carbohydrate bonding is most often used with glycoproteins or any other carbohydrate-containing substance; carbohydrate is used with lectins, glycoproteins, or any other carbohydrate metabolite protein.
1468:
Vassylyeva, Marina N.; Klyuyev, Sergiy; Vassylyev, Alexey D.; Wesson, Hunter; Zhang, Zhuo; Renfrow, Matthew B.; Wang, Hengbin; Higgins, N. Patrick; Chow, Louise T.; Vassylyev, Dmitry G. (27 June 2017).
414:
Monoclonal antibodies can also be selected to bind proteins with great specificity, where protein is released under fairly gentle conditions. This can become of use for further research in the future.
922:
Baur, Daniel; Angarita, Monica; Müller-Späth, Thomas; Steinebach, Fabian; Morbidelli, Massimo (2016). "Comparison of batch and continuous multi-column protein A capture processes by optimal design".
1717:
Naval, Javier; Calvo, Miguel; Lampreave, Fermin; Piñeiro, Andrés (1 January 1983). "Affinity chromatography of serum albumin: An illustrative laboratory experiment on biomolecular interactions".
1643:
2171:
1803:
Duong-Thi, M. D.; Meiby, E.; Bergström, M.; Fex, T.; Isaksson, R.; Ohlson, S. (2011). "Weak affinity chromatography as a new approach for fragment screening in drug discovery".
350:
Affinity chromatography can be used in a number of applications, including nucleic acid purification, protein purification from cell free extracts, and purification from blood.
504:
in order to aid their purification. The protein may have been genetically modified so as to allow it to be selected for affinity binding; this is known as a fusion protein.
2290:
389:
Speciality media are designed for a specific class or type of protein/co enzyme; this type of media will only work to separate a specific protein or coenzyme.
577:
from another glycoform. Although there are various ways to perform lectin affinity chromatography, the goal is extract a sugar ligand of the desired protein.
2166:
2638:
1061:
Mahmoudi Gomari, Mohammad; Saraygord-Afshari, Neda; Farsimadan, Marziye; Rostami, Neda; Aghamiri, Shahin; Farajollahi, Mohammad M. (1 December 2020).
2161:
2029:
1351:
J. D. Muller; C. R. Wilks; K. J. O'Riley; R. J. Condron; R. Bull; A. Mateczun (2004). "Specificity of an immunochromatographic test for anthrax".
339:
386:
Nucleic acids function to trap mRNA, DNA, rRNA, and other nucleic acids/oligonucleotides. Protein A/G method is used to purify immunoglobulins.
2120:
2115:
2100:
1647:
1409:
881:
41:
interaction between the biomolecule and another substance. The specific type of binding interaction depends on the biomolecule of interest;
793:
500:
Possibly the most common use of affinity chromatography is for the purification of recombinant proteins. Proteins with a known affinity are
1980:
1116:
610:. Clinical adaptations have applied this type of chromatography for use in determining long term assessment of diabetic patients through
334:
by changing salt concentrations, pH, pI, charge and ionic strength directly or through a gradient to resolve the particles of interest.
2283:
1556:
1037:
372:
89:
Affinity chromatography has the advantage of specific binding interactions between the analyte of interest (normally dissolved in the
73:
binding interactions are frequently exploited for isolation of various biomolecules. Affinity chromatography is useful for its high
1693:
1335:
1148:
906:
856:
828:
777:
678:
2448:
2105:
1063:"Opportunities and challenges of the tag-assisted protein purification techniques: Applications in the pharmaceutical industry"
2458:
2145:
2438:
2276:
2135:
2130:
1353:
2413:
2022:
654:
obtained retention times of analyzed compounds. Affinity chromatography is part of a larger suite of techniques used in
285:
94:
2488:
2473:
2238:
2231:
2085:
189:
78:
2508:
2075:
467:
97:). In a typical affinity chromatography experiment, the ligand is attached to a solid, insoluble matrix—usually a
1390:"Direct Capture of His6-Tagged Proteins Using Megaporous Cryogels Developed for Metal-Ion Affinity Chromatography"
74:
2548:
2433:
2224:
2140:
2054:
1999:
248:
2318:
2591:
1433:
Gaberc-Porekar, Vladka K.; Menart, Viktor (2001). "Perspectives of immobilized-metal affinity chromatography".
645:) is an affinity chromatography technique for affinity screening in drug development. WAC is an affinity-based
54:
681:(PPI) targets. WAC has been shown to be more effective than established methods for fragment based screening.
606:
Boronate affinity chromatography consists of using boronic acid or boronates to elute and quantify amounts of
485:
A chromatography column containing nickel-agarose beads used for purification of proteins with histidine tags
2643:
2358:
2257:
2049:
2015:
622:
Affinity purification of albumin and macroglobulin contamination is helpful in removing excess albumin and α
2453:
2383:
2197:
1062:
2573:
2568:
2373:
2333:
2187:
2090:
2080:
1277:"Automated On-Line Isolation and Fractionation System for Nanosized Biomacromolecules from Human Plasma"
62:
58:
2523:
2408:
2353:
2207:
2125:
1919:
1761:
1482:
1223:
897:
Fanali, Salvatore; Haddad, Paul R.; Poole, Colin F.; Schoenmakers, Peter; Lloyd, David, eds. (2013).
594:
978:
2343:
2192:
674:
611:
434:
1600:
379:
Hydrophobic interaction media are most commonly used to target free carboxyl groups and proteins.
298:
2403:
2299:
2202:
2110:
2095:
1785:
1578:
1257:
1098:
957:
750:
425:
residue is added at either the N- or C-terminus of the peptide. This cysteine residue contains a
2543:
2418:
2378:
1973:
1947:
1859:
1820:
1777:
1734:
1699:
1689:
1625:
1570:
1562:
1552:
1518:
1500:
1471:"Efficient, ultra-high-affinity chromatography in a one-step purification of complex proteins"
1450:
1415:
1405:
1370:
1331:
1308:
1249:
1195:
1154:
1144:
1090:
1082:
1043:
1033:
949:
902:
877:
852:
824:
773:
742:
690:
650:
490:
110:
38:
1994:
1937:
1927:
1851:
1812:
1769:
1726:
1615:
1544:
1508:
1490:
1442:
1397:
1362:
1298:
1288:
1239:
1231:
1185:
1136:
1074:
1008:
939:
931:
732:
724:
204:
141:
1894:
Affinity chromatography is a novel technique which was conceived by
Cuatrecasas and Wilchek
474:
the protein of interest include changing the pH, or adding a competitive molecule, such as
2601:
2538:
2463:
2443:
2423:
2398:
2338:
1396:. Methods in Molecular Biology. Vol. 1286. New York: Humana Press. pp. 201–212.
655:
1923:
1765:
1486:
1227:
2617:
2328:
2038:
1513:
1470:
1366:
1303:
1276:
646:
565:
438:
417:
A simplified strategy is often employed to purify antibodies generated against peptide
270:
251:
174:
106:
17:
1942:
1907:
1446:
1140:
2632:
2558:
2533:
1730:
1261:
1102:
1078:
961:
754:
470:
can be used to introduce such a protein tag into the relevant gene. Methods used to
2518:
2503:
2393:
2363:
1877:
1789:
1582:
1388:
Singh, Naveen K.; DSouza, Roy N.; Bibi, Noor S.; Fernández-Lahore, Marcelo (2015).
694:
607:
570:
184:
90:
70:
1548:
1401:
1389:
1293:
2493:
2348:
1969:"Affinity Chromatography Principle, Procedure And Advance Detailed Note – 2020".
1620:
627:
513:
505:
501:
243:
34:
1912:
Proceedings of the
National Academy of Sciences of the United States of America
1475:
Proceedings of the
National Academy of Sciences of the United States of America
2513:
2498:
2388:
2323:
1235:
426:
280:
230:
1816:
1781:
1738:
1703:
1566:
1504:
1086:
1047:
2596:
1495:
574:
546:
521:
509:
475:
446:
442:
265:
261:
1863:
1824:
1629:
1574:
1522:
1454:
1419:
1374:
1312:
1253:
1199:
1158:
1094:
953:
935:
746:
728:
1951:
1932:
1013:
481:
2553:
2528:
2313:
944:
666:
422:
154:
118:
in affinity chromatography procedures are summarized in the table below.
46:
1244:
2428:
2268:
737:
662:
517:
471:
418:
331:
199:
159:
102:
98:
66:
42:
1855:
1190:
1173:
406:
buffer such as glycine pH 2.8. The eluate is collected into a neutral
2368:
1773:
901:. Handbooks in Separation Science. Saint Louis: Elsevier. p. 3.
670:
561:
557:
537:
529:
525:
219:
214:
169:
50:
1968:
1686:
Fundamental laboratory approaches for biochemistry and biotechnology
1671:
Fundamental
Laboratory Approaches for Biochemistry and Biotechnology
770:
Fundamental
Laboratory Approaches for Biochemistry and Biotechnology
564:
are used to separate components within the sample. Lectins, such as
569:
D-N-acetyl-glucosamine. The most common application is to separate
560:
affinity chromatography is a form of affinity chromatography where
421:. When the peptide antigens are produced synthetically, a terminal
2563:
1275:
Multia E, Liangsupree T, Jussila M, et al. (September 2020).
305:
297:
2007:
661:
The WAC technology is demonstrated against a number of different
541:
533:
407:
306:
122:
Typical biological interactions used in affinity chromatography
2272:
2011:
1684:
Ninfa, Alexander J.; Ballou, David P.; Benore, Marilee (2010).
1669:
Ninfa, Alexander J.; Ballou, David P.; Benore, Marilee (2006).
768:
Ninfa, Alexander J.; Ballou, David P.; Benore, Marilee (2009).
689:
Affinity chromatography was conceived and first developed by
1752:
Zopf, D.; S. Ohlson (1990). "Weak-affinity chromatography".
1601:"Affinity Chromatography: A Review of Clinical Applications"
1539:
Freeze, H. H. (May 2001). "Lectin affinity chromatography".
1328:
Point-of-care testing: principles and clinical applications
520:
binding protein (MBP), and the
Colicin E7 variant CL7 tag.
403:
1908:"Selective enzyme purification by affinity chromatography"
1135:. Methods in Enzymology. Vol. 463. pp. 475–494.
851:(2nd ed.). Totowa, N.J.: Taylor & Francis Group.
823:(2nd ed.). Totowa, N.J.: Humana Press. pp. 1–2.
437:
have been purified using affinity chromatography based on
81:
of separation, compared to other chromatographic methods.
1688:(2nd ed.). Hoboken, N.J.: John Wiley. p. 240.
1906:
P Cuatrecasas; M Wilchek; C B Anfinsen (October 1968).
93:), and a binding partner or ligand (immobilized on the
327:
phase does not exit the column with the liquid phase.
383:
separate dehydrogenases, kinases, and transaminases.
1003:
Ahern, Kevin; Rajagopal, Indira (12 February 2015).
2610:
2582:
2481:
2306:
2216:
2180:
2154:
2063:
1534:
1532:
1644:"GE Healthcare Life Sciences, Immobilized lectin"
876:. New Delhi: Pathfinder Publication. p. 11.
2172:Pyrolysis–gas chromatography–mass spectrometry
973:
971:
821:Affinity Chromatography: Methods and Protocols
2284:
2023:
1836:
1834:
1543:. Vol. Chapter 9. pp. 9.1.1–9.1.9.
1330:. Berlin, Germany: Springer. pp. 71–72.
461:Immobilized metal ion affinity chromatography
8:
1594:
1592:
1007:(3rd ed.). DaVinci Press. p. 822.
794:""Introduction to Affinity Chromatography""
302:Principle of affinity column chromatography
109:—chemically modified to introduce reactive
37:from a mixture, based on a highly specific
2291:
2277:
2269:
2030:
2016:
2008:
1133:Guide to Protein Purification, 2nd Edition
1941:
1931:
1619:
1512:
1494:
1302:
1292:
1243:
1189:
1012:
943:
842:
840:
736:
480:
120:
2167:Liquid chromatography–mass spectrometry
706:
573:from non-glycosylated proteins, or one
340:periodic counter-current chromatography
27:Purification technique for biomolecules
2116:Micellar electrokinetic chromatography
2101:High-performance liquid chromatography
1028:Grisham, Charles M. (1 January 2013).
612:analysis of their glycated hemoglobin
7:
2162:Gas chromatography–mass spectrometry
1541:Current Protocols in Protein Science
1174:"Affinity as a tool in life science"
772:(2nd ed.). Wiley. p. 133.
1673:(2nd ed.). Wiley. p. 153.
899:Liquid Chromatography: Applications
1367:10.1111/j.1751-0813.2004.tb12682.x
658:based drug target identification.
25:
1974:"What is affinity chromatography"
1032:. Brooks/Cole, Cengage Learning.
2639:Biochemical separation processes
2472:
2253:
2252:
1878:"Meir Wilchek - Wolf Foundation"
1079:10.1016/j.biotechadv.2020.107653
874:Biophysics and Molecular Biology
819:Zachariou, Michael, ed. (2008).
602:Boronate affinity chromatography
2106:Capillary electrochromatography
2146:Two-dimensional chromatography
457:microbe causing an infection.
1:
2136:Size-exclusion chromatography
2131:Reversed-phase chromatography
1447:10.1016/S0165-022X(01)00207-X
1354:Australian Veterinary Journal
1141:10.1016/s0076-6879(09)63028-7
2000:Resources in other libraries
1731:10.1016/0307-4412(83)90004-3
1549:10.1002/0471140864.ps0901s00
1402:10.1007/978-1-4939-2447-9_16
1294:10.1021/acs.analchem.0c01986
1005:Biochemistry Free & Easy
847:Bonner, Philip L.R. (2007).
800:. Bio-Rad. 14 September 2020
639:Weak affinity chromatography
634:Weak affinity chromatography
286:polyhistidine fusion protein
222:/Biotin-conjugated molecule
33:is a method of separating a
2239:Journal of Chromatography B
2232:Journal of Chromatography A
2121:Normal-phase chromatography
2086:Displacement chromatography
679:protein–protein interaction
235:Calmodulin binding partner
190:Complementary base sequence
2660:
2509:Electrostatic precipitator
2076:Argentation chromatography
618:Serum albumin purification
524:tags have an affinity for
488:
468:recombinant DNA technology
2549:Rotary vacuum-drum filter
2470:
2248:
2225:Biomedical Chromatography
2141:Thin-layer chromatography
2045:
1995:Resources in your library
1621:10.1093/clinchem/45.5.593
1435:J Biochem Biophys Methods
1392:. In Reichelt, S. (ed.).
1236:10.1016/j.aca.2019.09.022
1117:"Affinity Chromatography"
649:technique that separates
449:, derived from bacteria.
2592:Aqueous two-phase system
2414:Liquid–liquid extraction
1817:10.1016/j.ab.2011.02.022
1599:Hage, David (May 1999).
354:many folds in one step.
330:Affinity columns can be
2489:API oil–water separator
2359:Dissolved air flotation
2071:Affinity chromatography
1986:Affinity chromatography
1805:Analytical Biochemistry
1496:10.1073/pnas.1704872114
1394:Affinity Chromatography
508:include hexahistidine (
338:processes are known as
294:Batch and column setups
31:Affinity chromatography
18:Affinity Chromatography
2454:Solid-phase extraction
2217:Prominent publications
2198:Kovats retention index
1216:Analytica Chimica Acta
1067:Biotechnology Advances
936:10.1002/biot.201500481
872:Kumar, Pranav (2018).
729:10.1002/elps.201700207
647:liquid chromatographic
516:-S-transferase (GST),
486:
358:Various affinity media
311:
303:
39:macromolecular binding
2574:Vacuum ceramic filter
2569:Sublimation apparatus
2374:Electrochromatography
2334:Cross-flow filtration
2188:Distribution constant
2091:Electrochromatography
2081:Column chromatography
1933:10.1073/pnas.61.2.636
1719:Biochemical Education
1326:Luppa, Peter (2018).
924:Biotechnology Journal
484:
435:monoclonal antibodies
309:
301:
2524:Fractionating column
2319:Acid–base extraction
2300:Separation processes
2208:Van Deemter equation
2126:Paper chromatography
1844:Analytical Chemistry
1281:Analytical Chemistry
849:Protein Purification
595:Alkaline phosphatase
590:Alkaline phosphatase
496:Recombinant proteins
310:Batch chromatography
2344:Cyclonic separation
2193:Freundlich equation
1924:1968PNAS...61..636C
1766:1990Natur.346...87Z
1487:2017PNAS..114E5138V
1481:(26): E5138–E5147.
1287:(19): 13058–13065.
1228:2019AcAC.1091..160M
123:
2404:Gravity separation
2155:Hyphenated methods
2111:Ion chromatography
2096:Gas chromatography
1608:Clinical Chemistry
651:chemical compounds
487:
312:
304:
142:Substrate analogue
121:
2626:
2625:
2544:Rapid sand filter
2439:Recrystallization
2419:Electroextraction
2379:Electrofiltration
2266:
2265:
1981:Library resources
1884:. 9 December 2018
1856:10.1021/ac400715t
1850:(14): 6756–6766.
1411:978-1-4939-2447-9
1191:10.2144/000112803
883:978-93-80473-15-4
691:Pedro Cuatrecasas
491:Polyhistidine-tag
291:
290:
111:functional groups
16:(Redirected from
2651:
2476:
2293:
2286:
2279:
2270:
2256:
2255:
2203:Retention factor
2032:
2025:
2018:
2009:
1956:
1955:
1945:
1935:
1903:
1897:
1896:
1891:
1889:
1874:
1868:
1867:
1838:
1829:
1828:
1800:
1794:
1793:
1774:10.1038/346087a0
1749:
1743:
1742:
1714:
1708:
1707:
1681:
1675:
1674:
1666:
1660:
1659:
1657:
1655:
1646:. Archived from
1640:
1634:
1633:
1623:
1605:
1596:
1587:
1586:
1536:
1527:
1526:
1516:
1498:
1465:
1459:
1458:
1441:(1–3): 335–360.
1430:
1424:
1423:
1385:
1379:
1378:
1348:
1342:
1341:
1323:
1317:
1316:
1306:
1296:
1272:
1266:
1265:
1247:
1210:
1204:
1203:
1193:
1172:Uhlén M (2008).
1169:
1163:
1162:
1127:
1121:
1120:
1113:
1107:
1106:
1058:
1052:
1051:
1025:
1019:
1018:
1016:
1000:
994:
993:
991:
989:
975:
966:
965:
947:
919:
913:
912:
894:
888:
887:
869:
863:
862:
844:
835:
834:
816:
810:
809:
807:
805:
790:
784:
783:
765:
759:
758:
740:
711:
373:Dye ligand media
133:Target molecule
130:Types of ligand
124:
95:stationary phase
21:
2659:
2658:
2654:
2653:
2652:
2650:
2649:
2648:
2629:
2628:
2627:
2622:
2606:
2584:
2578:
2539:Protein skimmer
2477:
2468:
2464:Ultrafiltration
2444:Reverse osmosis
2424:Microfiltration
2399:Froth flotation
2339:Crystallization
2302:
2297:
2267:
2262:
2244:
2212:
2176:
2150:
2059:
2041:
2036:
2006:
2005:
2004:
1989:
1988:
1984:
1965:
1960:
1959:
1905:
1904:
1900:
1887:
1885:
1882:Wolf Foundation
1876:
1875:
1871:
1840:
1839:
1832:
1802:
1801:
1797:
1760:(6279): 87–88.
1751:
1750:
1746:
1716:
1715:
1711:
1696:
1683:
1682:
1678:
1668:
1667:
1663:
1653:
1651:
1650:on 3 March 2012
1642:
1641:
1637:
1603:
1598:
1597:
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1559:
1538:
1537:
1530:
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1462:
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1431:
1427:
1412:
1387:
1386:
1382:
1350:
1349:
1345:
1338:
1325:
1324:
1320:
1274:
1273:
1269:
1212:
1211:
1207:
1171:
1170:
1166:
1151:
1129:
1128:
1124:
1115:
1114:
1110:
1060:
1059:
1055:
1040:
1027:
1026:
1022:
1002:
1001:
997:
987:
985:
977:
976:
969:
921:
920:
916:
909:
896:
895:
891:
884:
871:
870:
866:
859:
846:
845:
838:
831:
818:
817:
813:
803:
801:
792:
791:
787:
780:
767:
766:
762:
717:Electrophoresis
713:
712:
708:
703:
687:
656:chemoproteomics
636:
625:
620:
604:
592:
583:
555:
498:
493:
463:
395:
360:
348:
296:
271:Immunoglobulins
87:
28:
23:
22:
15:
12:
11:
5:
2657:
2655:
2647:
2646:
2644:Chromatography
2641:
2631:
2630:
2624:
2623:
2621:
2620:
2618:Unit operation
2614:
2612:
2608:
2607:
2605:
2604:
2599:
2594:
2588:
2586:
2580:
2579:
2577:
2576:
2571:
2566:
2561:
2556:
2551:
2546:
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2531:
2526:
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2501:
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2483:
2479:
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2471:
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2456:
2451:
2446:
2441:
2436:
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2426:
2421:
2416:
2411:
2406:
2401:
2396:
2391:
2386:
2381:
2376:
2371:
2366:
2361:
2356:
2351:
2346:
2341:
2336:
2331:
2329:Chromatography
2326:
2321:
2316:
2310:
2308:
2304:
2303:
2298:
2296:
2295:
2288:
2281:
2273:
2264:
2263:
2261:
2260:
2249:
2246:
2245:
2243:
2242:
2235:
2228:
2220:
2218:
2214:
2213:
2211:
2210:
2205:
2200:
2195:
2190:
2184:
2182:
2178:
2177:
2175:
2174:
2169:
2164:
2158:
2156:
2152:
2151:
2149:
2148:
2143:
2138:
2133:
2128:
2123:
2118:
2113:
2108:
2103:
2098:
2093:
2088:
2083:
2078:
2073:
2067:
2065:
2061:
2060:
2058:
2057:
2052:
2046:
2043:
2042:
2039:Chromatography
2037:
2035:
2034:
2027:
2020:
2012:
2003:
2002:
1997:
1991:
1990:
1979:
1978:
1977:
1976:
1971:
1964:
1963:External links
1961:
1958:
1957:
1918:(2): 636–643.
1898:
1869:
1830:
1811:(1): 138–146.
1795:
1744:
1709:
1694:
1676:
1661:
1635:
1614:(5): 593–615.
1588:
1558:978-0471140863
1557:
1528:
1460:
1425:
1410:
1380:
1361:(4): 220–222.
1343:
1336:
1318:
1267:
1205:
1164:
1149:
1122:
1108:
1053:
1039:978-1133106296
1038:
1020:
1014:10211.3/206119
995:
979:"Cube Biotech"
967:
930:(7): 920–931.
914:
907:
889:
882:
864:
857:
836:
829:
811:
785:
778:
760:
723:(2): 344–347.
705:
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702:
699:
686:
683:
635:
632:
623:
619:
616:
603:
600:
591:
588:
582:
579:
566:concanavalin A
554:
551:
502:protein tagged
497:
494:
462:
459:
439:immunoglobulin
394:
393:Immunoaffinity
391:
359:
356:
347:
344:
295:
292:
289:
288:
283:
278:
274:
273:
268:
259:
255:
254:
252:fusion protein
246:
241:
237:
236:
233:
228:
224:
223:
217:
212:
208:
207:
202:
197:
193:
192:
187:
182:
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177:
175:Polysaccharide
172:
167:
163:
162:
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147:
144:
139:
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134:
131:
128:
107:polyacrylamide
86:
83:
26:
24:
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13:
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9:
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2:
2656:
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2590:
2589:
2587:
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2575:
2572:
2570:
2567:
2565:
2562:
2560:
2559:Spinning cone
2557:
2555:
2552:
2550:
2547:
2545:
2542:
2540:
2537:
2535:
2534:Mixer-settler
2532:
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2449:Sedimentation
2447:
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2435:
2434:Precipitation
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1184:(5): 649–54.
1183:
1179:
1178:BioTechniques
1175:
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1150:9780123745361
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946:
945:11311/1013726
941:
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910:
908:9780124158061
904:
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858:9780415385114
854:
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843:
841:
837:
832:
830:9781588296597
826:
822:
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812:
799:
795:
789:
786:
781:
779:9780470087664
775:
771:
764:
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664:
659:
657:
652:
648:
644:
640:
633:
631:
629:
617:
615:
613:
609:
608:glycoproteins
601:
599:
596:
589:
587:
580:
578:
576:
572:
571:glycoproteins
567:
563:
559:
552:
550:
548:
543:
539:
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531:
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523:
519:
515:
511:
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409:
405:
399:
392:
390:
387:
384:
380:
377:
374:
368:
364:
357:
355:
351:
346:Specific uses
345:
343:
341:
335:
333:
328:
324:
320:
316:
308:
300:
293:
287:
284:
282:
279:
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269:
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100:
96:
92:
84:
82:
80:
76:
72:
68:
64:
60:
56:
52:
48:
44:
40:
36:
32:
19:
2519:Filter press
2504:Depth filter
2394:Flocculation
2364:Distillation
2237:
2230:
2223:
2070:
1985:
1915:
1911:
1901:
1893:
1886:. Retrieved
1881:
1872:
1847:
1843:
1808:
1804:
1798:
1757:
1753:
1747:
1722:
1718:
1712:
1685:
1679:
1670:
1664:
1652:. Retrieved
1648:the original
1638:
1611:
1607:
1540:
1478:
1474:
1463:
1438:
1434:
1428:
1393:
1383:
1358:
1352:
1346:
1327:
1321:
1284:
1280:
1270:
1245:10138/321264
1219:
1215:
1208:
1181:
1177:
1167:
1132:
1125:
1111:
1070:
1066:
1056:
1030:Biochemistry
1029:
1023:
1004:
998:
988:11 September
986:. Retrieved
983:Cube Biotech
982:
927:
923:
917:
898:
892:
873:
867:
848:
820:
814:
804:14 September
802:. Retrieved
797:
788:
769:
763:
720:
716:
709:
695:Meir Wilchek
688:
660:
642:
638:
637:
621:
605:
593:
584:
556:
506:Protein tags
499:
464:
455:
451:
432:
416:
413:
400:
396:
388:
385:
381:
378:
369:
365:
361:
352:
349:
336:
329:
325:
321:
317:
313:
185:Nucleic acid
116:
91:mobile phase
88:
71:nucleic acid
30:
29:
2494:Belt filter
2459:Sublimation
2349:Decantation
1654:29 November
1222:: 160–168.
798:bio-rad.com
738:1874/362143
628:thiocyanate
514:glutathione
244:Glutathione
75:selectivity
35:biomolecule
2633:Categories
2583:Multiphase
2514:Evaporator
2499:Centrifuge
2389:Filtration
2384:Extraction
2324:Adsorption
2314:Absorption
2064:Techniques
1725:(1): 5–8.
1073:: 107653.
701:References
675:chaperones
665:targets –
489:See also:
441:-specific
427:sulfhydryl
411:antibody.
281:Nickel-NTA
231:Calmodulin
79:resolution
2597:Azeotrope
2307:Processes
1782:0028-0836
1739:1879-1468
1704:420027217
1567:1934-3663
1505:0027-8424
1262:203147714
1103:226276355
1087:0734-9750
1048:777722371
962:205492204
667:proteases
581:Specialty
575:glycoform
547:imidazole
522:Histidine
476:imidazole
447:Protein G
443:Protein A
266:Protein G
262:Protein A
85:Principle
55:substrate
2611:Concepts
2602:Eutectic
2554:Scrubber
2529:Leachate
2409:Leaching
2354:Dialysis
2258:Category
2050:software
1888:17 March
1864:23806099
1825:21352794
1630:10222345
1575:18429210
1523:28607052
1455:11694288
1420:25749956
1375:15149073
1313:32893620
1254:31679569
1200:18474040
1159:19892188
1095:33157154
954:26992151
755:33657660
747:28905402
423:cysteine
419:antigens
205:Receptor
155:Antibody
146:Enzymes
101:such as
59:receptor
47:antibody
2585:systems
2482:Devices
2429:Osmosis
2055:history
1952:4971842
1920:Bibcode
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