Markussen J
Int J Pept Protein Res. 1985 Apr;25(4):431-4. doi: 10.1111/j.1399-3011.1985.tb02197.x.
The single chain des-(B30) insulin molecule (SCI) has been reduced and reoxidized together with porcine proinsulin (PPI). Yields of correctly folded and reoxidized SCI and PPI were analyzed by HPLC. The concentrations of both proteins were 10(-3) M during reduction and 10(-5) M during oxidation. The pH during reoxidation was varied from 8.6 to 9.2 and the temperature from 4 to 37 degrees. Under all conditions tested, the recovery of SCI was substantially higher than that of PPI. The recoveries peaked after 24-72 h. It is suggested that the "miniproinsulin" SCI folds correctly up more efficiently than porcine proinsulin, resulting in higher yields of reoxidized SCI.
单链去(B30)胰岛素分子(SCI)已与猪胰岛素原(PPI)一起进行还原和再氧化。通过高效液相色谱法(HPLC)分析正确折叠和再氧化的SCI和PPI的产率。还原过程中两种蛋白质的浓度均为10⁻³ M,氧化过程中为10⁻⁵ M。再氧化过程中的pH值在8.6至9.2之间变化,温度在4至37摄氏度之间变化。在所有测试条件下,SCI的回收率显著高于PPI。回收率在24 - 72小时后达到峰值。这表明“微型胰岛素原”SCI比猪胰岛素原更有效地正确折叠,从而导致再氧化的SCI产率更高。