TL;DR: Quantitative immunoprecipitation assays indicate that this specific protein represents 1% of the total soluble protein in the mouse olfactory bulb, and it is suggested that this protein is an example of selective genetic expression within the central nervous system.
Abstract: Soluble extracts from several regions of the mouse brain manifested regionally specific protein band patterns on polyacrylamide gel electrophoresis. In particular, one protein band appeared to occur uniquely in the olfactory bulb extracts where it was a quantitatively significant constituent of the soluble protein extract. This protein was purified to homogeneity by ammonium sulfate precipitation, DEAE-cellulose column chromatography, and polyacrylamide gel electrophoresis. The purified protein has a minimum molecular weight of about 20,000 by gel electrophoresis in the presence of sodium dodecyl sulfate. Precipitating antiserum prepared against this protein reacted only with the purified protein or with extracts of olfactory bulb, and not with extracts of other mouse tissues or brain regions. Quantitative immunoprecipitation assays indicate that this specific protein represents 1% of the total soluble protein in the mouse olfactory bulb. Soluble extracts of olfactory bulbs from several rodent species gave reactions of identity by agar gel diffusion with the antiserum to the mouse protein. It is suggested that this protein is an example of selective genetic expression within the central nervous system.
TL;DR: A lymphoid-cell specific surface membrane antigen of the mouse has been purified over 200-fold by differential solubilization, ion exchange chromatography and gel filtration and revealed a single strong band of precipitation, whereas no immunoprecipitation could be detected in conventional—or crossing-over immunoelectrophoresis.
Abstract: A lymphoid-cell specific surface membrane antigen of the mouse has been purified over 200-fold by differential solubilization, ion exchange chromatography and gel filtration. The serologic activity corresponded to a fraction of 67,000 molecular weight. Two main protein bands could be detected in acrylamide gel electrophoresis together with a very faint third band. Double gel diffusion revealed a single strong band of precipitation, whereas no immunoprecipitation could be detected in conventional—or crossing-over immunoelectrophoresis. This discrepancy is discussed. The antigen was strongly expressed on cells having an organ distribution similar to bone marrow-derived cells and slightly expressed on a subpopulation of cells which was similarly abundant in all lymphoid organs tested. During ontogeny the antigen was strongly expressed on thymocytes with a transient maximum between days 4 and 8 after gestation.