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A comparative investigation was made of the protein composition of structures of the rat brain (premotor cortex, area CA3 of the hippocampus, caudate nucleus, frontal lobe of the cerebellum) by electrophoresis in a continuous gradient of polyacrylamide gel (PAG) pores in capillary tubes. This method was shown to have much greater resolving power than electrophoresis in a uniform gel concentration. The method did not reveal any differences in the protein composition of the brain structures studied.

By a combination of microelectrophoresis and precipitation in polyacrylamide gel, α-fetoprotein (α-FP) produced by single hepatocytes and by microcolonies of hepatocytes was determined. Liver cells from 6–13-week-old human fetuses were cultivatedin vitro for 2–5 days. α-FP was found to be produced in amounts of between 70 and 800 pg per cell by 23 of 28 single hepatocytes and by 89 of 91 microcolonies consisting of 2 to 35 cells

The diffusion and ζ potentials of red cells in blood flowing directly from a zone of myocardial ischemia along a branch of the great cardiac vein in the acute period of experimental infarction were studied by a microelectrode method and by microelectrophoresis. By this means the energy of electrostatic repulsion (EER) between the blood cells to be calculated and factors exerting a significant effect on this parameter in acute experimental myocardial infarction caused by ligation of the anterior interventricular branch of the left coronary artery in 20 dogs could be identified. The energetic state of the double electric layer was shown to be a leading factor in the change in EER and manifestation of the aggregation properties of the blood cells. A statistically significant decrease in the energetic potentials of the red cells was found in blood taken directly from the zone of myocardial ischemia.

A modified technique of agar electrophoresis is suggested; this method is applicable to the study of microquantities of solutions with low protein content. The technique allows the analysis to be made of the fraction protein composition of such biological fluids as aqueous humor of the eye and internal ear perilymph. The findings relating to the fluids under normal and pathological conditions are presented.

A simple method is suggested for fractionation of acid proteins. The method sensitivity is 10(-11) g per single band. Since the available modifications of capillary microelectrophoresis are very complicated to apply to an analysis of protein picograms, such a method was badly needed. Fractionation of the samples is made on polyacrylamide gel tubes up to 40 microns in diameter. An original buffer system is employed. The possibility of fractionating acid proteins from vertebrate animal brain has been demonstrated.

An electrophoretic analysis of the dissolved precipitate and supernatant fluid was conducted in the equivalent zone. For microelectrophoresis on paper, a Flynn and De Mayo type of chamber as modified by A. E. Gurvich was used. The specific precipitate, thoroughly washed with saline solution, largely consists of the γ-globulins of the immune serum (about 85%) and proteins, the electrophoretic mobility of which approaches that of the β2 and β-globulins. Albumins adsorbed by the specific antigen-antibody complex are lost in washing the precipitate. A suggestion is made that about 15% of the precipitate consists of nonspecific proteins.

A simple cuvette is described which is to be used for serial analyses by means of modified micromethods of electrophoresis on agar and starch gel immune electrophoresis on agar. The instrument can be made in any laboratory.