Immunoaffinity chromatography applications

A. Bronshtein, N. Aharonson, A. Turniansky, and M. Altstein, Sol-gel-based immunoaffinity chromatography application to nitroaromatic compounds. Chem. Mater. 12, 2050-2058 (2000). 

Sanchez-Martinez, M., M. Aguilar-Caballos, S. Eremin, et al. 2006. Long-wavelength fluorimetry as an indirect detection system in immunoaffinity chromatography Application to environmental analysis. Anal. Bioanal.Chem. 386 1489-1495. 

Downham, M., Busby, S., Jefferis, R., and Lyddiatt, A., Immunoaffinity chromatography in biorecovery an application of recombinant DNA technology to generic adsorption processes, /. Chromatogr., 584, 59, 1992. 

McConnell RJ, Fitzgerald SP, Lamont JV (1992) Trenbolone and 19-nortestosterone residue analysis by immunoaffinity chromatography and high-performance liquid chromatography and/or an enzyme-linked immunosorbent assay. In Morgan MRA, Smith CJ, Williams PA (eds) Food safety and quality assurance applications of immunoassay systems. Elsevier, Barking, p 245... 

Hage, D. S., Survey of recent advances in analytical applications of immunoaffinity chromatography. Journal of Chromatography. B, Biomedical Sciences and Applications 715(1), 3-28, 1998. 

Immunoaffinity chromatography cleanup has also been applied as an ideal and reliable strategy for residue analysis. Immunoaffinity columns prepared by coupling the antibodies to a cyanogen bromide-activated support were used to analyze avermectin BI residues in cattle tissues (359) and ivermectin in sheep serum (376). An immunoaffinity column prepared by an alternative activation/ coupling procedure with carbonyl diimidazole was also employed to analyze ivermectin residues in swine liver (361) since the earlier-reported methods did not work well in the analysis of this matrix. This recent work demonstrated the high specificity of tire antibody-mediated cleanup, but also showed that the immunoaffinity procedures could not always or completely eliminate matrix interference of samples. Therefore, application of additional cleanup steps before or after these procedures is often inevitable. 

H Zou, Y Zhang, P Lu, and IS Krull. Perfusion immunoaffinity chromatography and its application in analysis and purification of biomolecules. Biomed Chromatography 10 122-126, 1996. 

Immunoaffinity chromatography can provide extensive purification of endogenous hormones in plant extracts [60] (see Figs. 6 and 7 in Section 6.2). Both monoclonal and polyclonal antibodies have been used to produce immunoaffinity supports for lAA [60,61], GAs [62,63] and cytokinins [64,65]. Despite the enormous potential of the procedure, it has as yet not found widespread application in plant hormone purification protocols. The situation is unlikely to change until a range of immunoaffinity supports are available from commercial sources at affordable prices. The raising of antibodies against plant hormones, the preparation of a variety of immunoaffinity supports and their application in plant hormone analysis are discussed and evaluated in Chapter 3. 

In view of the data obtained when extracts from P. sylvestris and D. dolichopetala were purified by immunoaffinity chromatography and analysed by ion-suppression, reverse phase HPLC, it would have been very tempting to assume that the application of these procedures to the analysis of extracts from dwarf-1 Zea mays, and other tissues, would also provide accurate quantitative estimates of endogenous lAA. The HPLC trace illustrated in Fig. 8B, in which a Gaussian-shaped fluorescent lAA-like peak is a major component, would appear to support this belief. However, the data in Fig. 8C show that such an assumption would have been incorrect and led to an inaccurate overestimate of lAA. 

Serum Albumin Another application of the immunoaffinity chromatography technique was in the analysis of AFBl bound to serum albumin (9). Blood samples were collected on Day 5 from the same individuals who participated in the study described above. Serum albumin was selectively isolated from blood and subjected to enzymatic proteolysis using Pronase. Aflatoxin specific adducts were purified by immu-noaffinity chromatography and quantified by competitive radioimmunoassay. A highly significant correlation of adduct level with AFBl intake (r = 0.69, P less than 0.000001) was observed. From the slope of the regression... 

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