Cupo J F, Lidgard G P, Lichtman W F
BASF Bioresearch Corporation, Cambridge, MA 02139.
Electrophoresis. 1990 Jun;11(6):500-4. doi: 10.1002/elps.1150110612.
An improved two-dimensional gel electrophoresis procedure has been developed utilizing isolated nuclear matrix proteins. The proteins of the cellular nuclear matrix are tissue specific. They are an example of a protein set whose two-dimensional electrophoretic patterns afford much information of clinical significance. However, current two-dimensional gel techniques were not completely satisfactory for the small amounts of protein present in tissue samples. There was a need for a two-dimensional gel procedure which was capable of increased sensitivity and resolution and at the same time was reliable and reproducible. This has been accomplished by implementing several modifications to the current two-dimensional gel procedures. In addition, changes were introduced in the silver staining process of the gels to increase the signal to background ratio. The overall procedure affects a dramatic increase in the resolution and clarity of the proteins visualized on two-dimensional gels and is no more laborious than current techniques.
利用分离出的核基质蛋白，已开发出一种改进的二维凝胶电泳方法。细胞核基质的蛋白质具有组织特异性。它们是一类蛋白质的实例，其二维电泳图谱能提供许多具有临床意义的信息。然而，对于组织样本中存在的少量蛋白质，目前的二维凝胶技术并不完全令人满意。需要一种二维凝胶方法，它能够提高灵敏度和分辨率，同时可靠且可重复。这已通过对当前二维凝胶方法进行若干改进得以实现。此外，在凝胶的银染过程中引入了变化，以提高信号与背景的比率。整个过程显著提高了二维凝胶上可视化蛋白质的分辨率和清晰度，并且并不比现有技术更费力。
