Large-scale isolation of equine liver alcohol dehydrogenase on a blue agarose gel
- 1 May 1979
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 21 (5), 775-785
- https://doi.org/10.1002/bit.260210504
Abstract
Equine liver alcohol dehydrogenase (EC 1.1.1.1) has been purified by a new scheme using a blue agarose gel (Blue Sepharose) as an affinity sorbent. Starting amounts of 0.6 to 10 kg liver have been processed to enzyme possessing 1.5 U/mg average specific activity, in about three to four days. Some parameters concerning adsorption of enzyme to the blue gel as well as recovery therefrom have been explored.This publication has 9 references indexed in Scilit:
- Use of blue dextran as a probe for the Nicotinamide Adenine Dinucleotide domain in proteinsAccounts of Chemical Research, 1977
- Observations on the effect of bicarbonate on the stability of horse liver alcohol dehydrogenaseInternational Journal of Biochemistry, 1977
- Blue sepharose: a reusable affinity chromatography medium for purification of alcohol dehydrogenaseBiochemical and Biophysical Research Communications, 1976
- Preparative purification of homogeneous steroid-active isozyme of horse liver alcohol dehydrogenase by affinity chromatography on an immobilized AMP-analogAnalytical Biochemistry, 1975
- Blue dextran-sepharose: an affinity column for the dinucleotide fold in proteins.Proceedings of the National Academy of Sciences of the United States of America, 1975
- Affinity Chromatography of Kinases and Dehydrogenases on Sephadex® and Sepharose® Dye DerivativesAdvances in experimental medicine and biology, 1974
- Structural and functional zinc in horse liver alcohol dehydrogenase.Proceedings of the National Academy of Sciences, 1967
- On the Purification of Liver Alcohol Dehydrogenase.Acta Chemica Scandinavica, 1958
- ZINC, A COMPONENT OF YEAST ALCOHOL DEHYDROGENASEProceedings of the National Academy of Sciences of the United States of America, 1955