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% 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.
Biochemical Separation Centre, University of Uppsala, Sweden.
G
G
Chaga
L
L
Andersson
B
B
Ersson
J
J
Porath
D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D005290:Ferric Compounds; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification*; D009132:Muscles / Q000201:enzymology*; D006005:Phosphorylases / Q000302:isolation & purification*
D005290:Ferric Compounds; D007770:L-Lactate Dehydrogenase; D006005:Phosphorylases