Membrane filtration affinity purification (MFAP) of dehydrogenases using cibacron blue
- 5 December 1989
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 34 (10) , 1321-1325
- https://doi.org/10.1002/bit.260341010
Abstract
The method for purification of biomolecules by a combination of affinity interactions and membrane filtration for separation of unwanted material has been found to be of interest for large‐scale work. This study examines the suitability of silica nanoparticles as carriers in the process. Alcohol dehydrogenase and lactate dehydrogenases were chosen as target molecules to be purified. The binding capacity was found to be comparative to what is obtained for high‐performance liquid chromatography (HPLC) packing material. Both binding and desorption of the enzymes were found to be effective. The limiting factor of the process was the filtration flow rate.This publication has 8 references indexed in Scilit:
- Synthesis and characterization of a water-soluble affinity polymer for trypsin purificationBiotechnology & Bioengineering, 1988
- Separation of trypsin from trypsin ?-chymotrypsin mixture by affinity-ultrafiltrationBiotechnology Letters, 1986
- [2] Immobilization of ligands with organic sulfonyl chloridesPublished by Elsevier ,1984
- Ultrafiltration affinity purificationJournal of Chromatography A, 1984
- Biospecific ultrafiltration: A promising purification technique for proteins?Journal of Membrane Science, 1981
- Protein purification using immobilised triazine dyesJournal of Chromatography A, 1979
- The specific interaction of Cibacron and related dyes with cyclic nucleotide phosphodiesterase and lactate dehydrogenaseBiochemical Journal, 1978
- Calorimetric investigation of NAD binding to some dehydrogenasesBiochemical and Biophysical Research Communications, 1977