Literature DB >> 11876301

Dye-ligand affinity adsorbents for enzyme purification.

N E Labrou1.   

Abstract

Affinity chromatography is widely employed in laboratory and large-scale for the purification of biotherapeutics and diagnostics. Some of the most widely used ligands in affinity chromatography have been several reactive chlorotriazine dyes. In particular, immobilized anthraquinone dyes have found a plethora of applications in affinity chromatography because they are inexpensive, are resistant to chemical and biological degradation, are sterilizable and cleanable in situ, and are readily immobilized to generate affinity adsorbents which display high binding capacity for a broad spectrum of proteins. This article provides detailed protocols on the preparation of a dye-ligand affinity adsorbent. Also, detailed protocols for effective application of these media, emphasizing binding and elution conditions are presented.

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Year:  2002        PMID: 11876301     DOI: 10.1385/MB:20:1:077

Source DB:  PubMed          Journal:  Mol Biotechnol        ISSN: 1073-6085            Impact factor:   2.695


  17 in total

Review 1.  Biomimetic dyes as affinity chromatography tools in enzyme purification.

Authors:  Y D Clonis; N E Labrou; V P Kotsira; C Mazitsos; S Melissis; G Gogolas
Journal:  J Chromatogr A       Date:  2000-09-01       Impact factor: 4.759

2.  Biomimetic-dye affinity chromatography for the purification of mitochondrial L-malate dehydrogenase from bovine heart.

Authors:  N E Labrou; Y D Clonis
Journal:  J Biotechnol       Date:  1996-03-08       Impact factor: 3.307

3.  Molecular modeling for the design of a biomimetic chimeric ligand. Application to the purification of bovine heart L-lactate dehydrogenase.

Authors:  N E Labrou; E Eliopoulos; Y D Clonis
Journal:  Biotechnol Bioeng       Date:  1999-05-05       Impact factor: 4.530

Review 4.  The affinity technology in downstream processing.

Authors:  N Labrou; Y D Clonis
Journal:  J Biotechnol       Date:  1994-08-15       Impact factor: 3.307

5.  L-Malate dehydrogenase from Pseudomonas stutzeri: purification and characterization.

Authors:  N E Labrou; Y D Clonis
Journal:  Arch Biochem Biophys       Date:  1997-01-01       Impact factor: 4.013

6.  Dye affinity labelling of yeast alcohol dehydrogenase.

Authors:  N E Labrou
Journal:  J Enzyme Inhib       Date:  2000

Review 7.  Application of bioaffinity technology in therapeutic extracorporeal plasmapheresis and large-scale fractionation of human plasma.

Authors:  T Burnouf; H Goubran; M Radosevich
Journal:  J Chromatogr B Biomed Sci Appl       Date:  1998-09-11

8.  Biomimetic-dye affinity adsorbents for enzyme purification: application to the one-step purification of Candida boidinii formate dehydrogenase.

Authors:  N E Labrou; A Karagouni; Y D Clonis
Journal:  Biotechnol Bioeng       Date:  1995-11-05       Impact factor: 4.530

9.  Design and applications of biomimetic anthraquinone dyes. Purification of calf intestinal alkaline phosphatase with immobilised terminal ring analogues of C.I. reactive blue 2.

Authors:  N M Lindner; R Jeffcoat; C R Lowe
Journal:  J Chromatogr       Date:  1989-06-28

10.  Affinity labelling of enzymes with triazine dyes. Isolation of a peptide in the catalytic domain of horse-liver alcohol dehydrogenase using Procion blue MX-R as a structural probe.

Authors:  D A Small; C R Lowe; T Atkinson; C J Bruton
Journal:  Eur J Biochem       Date:  1982-11
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