Use of immobilized metal ions as a negative adsorbent for purification of enzymes: application to phosphoglycerate mutase from chicken muscle extract and horseradish peroxidase.
Two enzymes, phosphoglycerate mutase and peroxidase, were purified by using an immobilized metal ion adsorbent for the removal of unwanted proteins. The mutase was obtained pure from a single column, whereas the purification of peroxidase required the use of a thiophilic adsorbent in a tandem. The capacity was 2.5 mg pure peroxidase per mL gel.
Chaga
G
G
Biochemical Separation Centre, Uppsala University, Sweden.
Andersson
L
L
Ersson
B
B
Berg
M
M
D000327:Adsorption; D000818:Animals; D001731:Bisphosphoglycerate Mutase / Q000302:isolation & purification*; D002412:Cations; D002645:Chickens; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006735:Horseradish Peroxidase / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008670:Metals; D009132:Muscles / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet
D002412:Cations; D008670:Metals; D006735:Horseradish Peroxidase; D001731:Bisphosphoglycerate Mutase