Purification of Two Muscle Enzymes by Chromatography on Immobilized Ferric Ions
- 1 August 1989
- journal article
- research article
- Published by Wiley in Biotechnology and Applied Biochemistry
- Vol. 11 (4) , 424-431
- https://doi.org/10.1111/j.1470-8744.1989.tb00068.x
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.This publication has 6 references indexed in Scilit:
- Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatographyAnalytical Biochemistry, 1986
- Fe3+-hydroxamate as immobilized metal affinity-adsorbent for protein chromatographyJournal of Chromatography A, 1985
- Immobilized metal affinity adsorption and immobilized metal affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ionsBiochemistry, 1983
- A Simple Procedure for the Isolation of Seven Abundant Muscle EnzymesPreparative Biochemistry, 1981
- Structural adaptations of lactate dehydrogenase isozymes.Proceedings of the National Academy of Sciences, 1977
- On the Role of Pyridoxal 5'-Phosphate in Phosphorylase. I. Absence of Classical Vitamin B6—dependent Enzymatic Activities in Muscle Glycogen Phosphorylase*Biochemistry, 1965