Karcher D, Lowenthal A, Van Soom G
Acta Neurol Belg. 1979 Jul-Aug;79(4):335-7.
There is a need for new methods to study CSF proteins. Kerenyi et al., 1973 and Verheecke, 1975 have already used this method and discussed its advantages. The electrophoresis is carried out according to the method of Wieme with as supporting medium agar. The volume applied varies between 5 to 15 microliters according to the total protein content and the width of the slit. Care must be taken to work at all times with bidistilled water and pro analysis reagents. After drying, the electrophoretic plates are reduced in a 10% solution of thiodiglycol, dried again, then immersed in 2% potassium hexacyanoferrate, washed thoroughly, then revealed with a silver nitrate solution (Kerenyi et al., 1973; Verheecke P., 1975) and left in 1% acetic acid. This technique is of major value as: 1. It avoids artefacts due to concentration and loss of proteins; 2. It works with very small amounts of fluid; 3. Where the CSF is silent for antibodies restricted heterogeneity using the classical methods, it reveals marked IgG fractionation.
需要有新的方法来研究脑脊液蛋白。凯伦伊等人(1973年)和韦尔赫克(1975年)已经使用了这种方法并讨论了其优点。电泳按照维姆的方法进行,以琼脂作为支持介质。根据总蛋白含量和狭缝宽度,加样体积在5至15微升之间变化。必须始终使用双蒸水和分析纯试剂。干燥后,将电泳板在10%的硫代二甘醇溶液中还原,再次干燥,然后浸入2%的铁氰化钾中,充分洗涤,然后用硝酸银溶液显色(凯伦伊等人,1973年;韦尔赫克P.,1975年),并置于1%的乙酸中。这项技术具有重要价值,因为:1. 它避免了由于蛋白质浓缩和损失导致的假象;2. 它适用于极少量的液体;3. 在使用经典方法脑脊液中抗体受限异质性不明显时,它能显示出明显的IgG分级分离。