Electrophoretic studies on solubilized proteins of goldfish brain

Abstract

Soluble proteins from homogenates of various regions of goldfish brain have been separated by gel electrophoresis techniques. Distribution of radioactive proteins formed following injection of a labeled amino acid was studied by direct autoradiography of gel slabs. While dye staining and labeling patterns of electrophoretically separated proteins did not vary among brain regions examined, there were marked differences in the positionh of stained bands and those detected autradiographically, suggesting diverse rates of metabolism of these soluble proteins. Unlike the protein staining and labeling patterns, the distribution of multiple electrophoretic bands of solubilized acetylcholinesterase varied among the 5 brain regions examined. Protein bands detected either by dye staining, autoradiography or by acetylcholinesterase activity did not vary measurably as a result of shock-avoidance training of the goldfish. In further studies with DFP, apparent turnover rates for the multiple forms of acetylcholinesterase in a detergent extract of whole brain were determined.