Song J L, Wang C C
National Laboratory of Macromolecules, Academia Sinica, Beijing, China.
Eur J Biochem. 1995 Jul 15;231(2):312-6. doi: 10.1111/j.1432-1033.1995.tb20702.x.
Protein disulfide-isomerase (PDI) in near stoichiometric concentrations promotes reactivation and prevents aggregation of guanidine-hydrochloride-denatured rhodanese during refolding upon dilution. PDI also suppresses aggregation of rhodanese during thermal inactivation. The above-mentioned properties displayed by PDI completely satisfy the definition of chaperone and provide additional evidence to confirm the hypothesis proposed previously [Wang, C. C. & Tsou, C. L. (1993) FASEB J. 7, 1515-1517] that PDI is both an enzyme and a chaperone. Since rhodanese contains no disulfide bonds, the chaperone-like activity of PDI acting on rhodanese is independent of its disulfide-isomerase activity.
接近化学计量浓度的蛋白质二硫键异构酶（PDI）在稀释复性过程中可促进盐酸胍变性的硫氰酸酶重新激活，并防止其聚集。PDI还能抑制硫氰酸酶在热失活过程中的聚集。PDI所表现出的上述特性完全符合伴侣蛋白的定义，并为先前提出的假设[Wang, C. C. & Tsou, C. L. (1993) FASEB J. 7, 1515 - 1517]提供了额外证据，即PDI既是一种酶又是一种伴侣蛋白。由于硫氰酸酶不含二硫键，PDI作用于硫氰酸酶的伴侣蛋白样活性与其二硫键异构酶活性无关。
