ELECTROPHORETIC PATTERNS OF EXTRACTABLE PROTEINS AND ENZYMES IN EMBRYONIC AND ADULT BRAINS

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Abstract
Extraction of soluble proteins from human embryonic and adult brains is described. Two different procedures are employed: Extraction with NaCl and with n-butanol, releasing proteins and enzymes associated with insoluble particles of the cells into solution. On agar-gel microelectrophoresis of the extracts 12-16 protein-fractions were separated in the embryonic extracts, 13-17 in the adult ones. Esterase activity was demonstrated on the electrophoresis by means of beta-naphthylacetate. In saline extracts of embryos 8-19 weeks old one dominant fraction shows esterase activity in the alpha area, while brains over 26 weeks and adult brains show 4 anodic and 6 sharp cathodic fractions. Preliminary inhibition tests with di-isopropyl-fluorophosphate, eserine and prostigmine 10-4 m were carried out. One crescent shaped anodic esterase and 2 cathodic esterases were completely inhibited by eserine 10-4, indicating the presence of one plasma- and two acetylcholinesterases. The esterase activity of embryos with alpha mobility was resistant to DFP. Alkaline phosphatase activity was demonstrable in n-butanol extracts only. The level of activity was found to be higher in a 13 weeks embryo than in 26 weeks and in adult brain extracts. 5 bands of lactate dehydrogenase isozymes were found in all brain extracts. Compared to adult whole brain fetal extracts showed higher activity in bands 3 and 4, and lower activity in bands 1, 2 and 5. Acid mucopolysaccharides were visualized on paper-electrophoresis.