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D Karcher

Publications and source records attributed to D Karcher.

57 records · Page 4Linked to original sources

Comparison of the brain specific protein alpha-albumin and GFA (glial fibrillary acidic protein).

In this study, the brain specific proteins alpha-albumin and glial fibrillary acidic protein (GFA) are compared by several biochemical and immunological methods. It is concluded that alpha-albumin and GFA are immunologically identical and biochemically narrowly related. The existence of two forms of this protein, a water soluble and a water insoluble, under physiological conditions is discussed by comparing the results of quantitative determinations and histoimmunological localizations.

Albumins↗

Cerebrospinal fluid protein electrophoresis without prior concentration.

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 microliter 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.

Animals↗

Cerebrospinal fluid proteins electrophoresis without prior concentration.

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.

Cerebrospinal Fluid Proteins↗