Abstract
Two enzymes, glycogen phosphorylase and lactate dehydrogenase, were purified simultaneously in a single step. Ferric ions immobilized on a chelating gel were used as the adsorbent. Adsorption and desorption steps were accomplished by changes in buffer composition. The recoveries were better than 80% and the capacities were about 5 mg of protein per milliliter of adsorbent. The procedure worked well both on a small and on a preparative scale. The homogeneity of the purified enzymes was checked by FPLC.
Dates
Type | When |
---|---|
Created | 1 year, 10 months ago (Oct. 20, 2023, 10:41 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 20, 2023, 10:42 p.m.) |
Indexed | 1 year, 5 months ago (March 24, 2024, 6:19 a.m.) |
Issued | 36 years ago (Aug. 1, 1989) |
Published | 36 years ago (Aug. 1, 1989) |
Published Online | 14 years, 8 months ago (Dec. 23, 2010) |
Published Print | 36 years ago (Aug. 1, 1989) |
@article{Chaga_1989, title={Purification of Two Muscle Enzymes by Chromatography on Immobilized Ferric Ions}, volume={11}, ISSN={1470-8744}, url={http://dx.doi.org/10.1111/j.1470-8744.1989.tb00068.x}, DOI={10.1111/j.1470-8744.1989.tb00068.x}, number={4}, journal={Biotechnology and Applied Biochemistry}, publisher={Wiley}, author={Chaga, G. and Andersson, L. and Ersson, B. and Porath, J.}, year={1989}, month=aug, pages={424–431} }