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 & Kiv...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical journal 1987-10, Vol.247 (1), p.237-239
Main Authors: Koivu, J, Myllylä, R, Kivirikko, K I
Format: Article
Language:English
Subjects:
Animals
Chick Embryo
Chromatography, Affinity
Chromatography, DEAE-Cellulose
Electrophoresis, Polyacrylamide Gel
Isomerases - isolation & purification
Protein Disulfide-Isomerases
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2470237