Koivu J, Myllylä R, Kivirikko K I
Department of Medical Biochemistry, University of Oulu, Finland.
Biochem J. 1987 Oct 1;247(1):237-9. doi: 10.1042/bj2470237.
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.
描述了一种用于纯化蛋白质二硫键异构酶（PDI）的两步法。该方法基于先前的发现，即脯氨酰4-羟化酶四聚体（α2β2）的β亚基与PDI相同[科伊武、米利拉、赫拉阿科斯奇、皮尔亚耶尼米、塔萨宁和基维里科（1987年）《生物化学杂志》262卷，6447 - 6449页；皮尔亚耶尼米、赫拉阿科斯奇、塔萨宁、米利拉、胡塔拉、科伊武和基维里科（1987年）《欧洲分子生物学组织杂志》6卷，643 - 649页]。该方法包括通过简单的亲和色谱法纯化脯氨酰4-羟化酶四聚体，随后通过离子交换色谱法从解离的四聚体中分离出β亚基。
