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自牛肝中纯化二硫键异构酶（PDI）。经匀浆、热沉淀、硫酸铵分级分离、阳离子和阴离子交换层析等步骤，得到了比活950U／g电泳纯的PDI。在此基础上研究了PDI对重组人粒／单系集落刺激因子（rhGM－CSF）体外复性作用。结果表明，在PDI与rhGM－CSF摩尔比为2：1时，可使0．5mg／ml的rhGM－CSF正确折叠率提高到60％，比活性由5．0×106U／mg提高到1．0×107U／mg。
Disulfide isomerase (PDI) was purified from bovine liver. After homogenization, thermal precipitation, ammonium sulfate fractionation, cation and anion exchange chromatography and other steps, a specific activity of 950U / g electrophoretic pure PDI was obtained. On the basis of this study, we investigated the renaturation effect of recombinant human granulocyte / monocyte-derived colony stimulating factor (rhGM-CSF) in vitro. The results showed that when the molar ratio of PDI to rhGM-CSF was 2: 1, the correct folding rate of 0.5mg / ml rhGM-CSF was increased to 60% and the specific activity increased from 5.0 × 106U / mg to 1. 0 × 107U / mg.