Purification of two muscle enzymes by chromatography on immobilized ferric ions

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%...

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Bibliographic Details
Published inBiotechnology and applied biochemistry Vol. 11; no. 4; p. 424
Main Authors Chaga, G, Andersson, L, Ersson, B, Porath, J
Format Journal Article
LanguageEnglish
Published United States 01.08.1989
Subjects
Animals
Chickens
Chromatography, Affinity
Ferric Compounds
L-Lactate Dehydrogenase - isolation & purification
Muscles - enzymology
Phosphorylases - isolation & purification
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Summary: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.
ISSN:0885-4513
DOI:10.1111/j.1470-8744.1989.tb00068.x