A simple procedure for the isolation of protein disulphide-isomerase.
A two-step procedure is described for the purification of protein disulphide-isomerase (PDI). This procedure is based on the previous finding that the beta-subunit of the prolyl 4-hydroxylase tetramer (alpha 2 beta 2) is identical with PDI [Koivu, Myllylä, Helaakoski, Pihlajaniemi, Tasanen & Kivirikko (1987) J. Biol. Chem. 262, 6447-6449; Pihlajaniemi, Helaakoski, Tasanen, Myllylä, Huhtala, Koivu & Kivirikko (1987) EMBO J. 6, 643-649]. The procedure involves purification of the prolyl 4-hydroxylase tetramer by a simple affinity chromatography and subsequent isolation of the beta-subunit from the dissociated tetramer by ion-exchange chromatography.
Koivu
J
J
Department of Medical Biochemistry, University of Oulu, Finland.
Myllylä
R
R
Kivirikko
K I
KI
D000818:Animals; D002642:Chick Embryo; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D007535:Isomerases / Q000302:isolation & purification*; D019704:Protein Disulfide-Isomerases
D007535:Isomerases; D019704:Protein Disulfide-Isomerases