Abstract
Primary explants of chick embryo intestine, cultivated in embryo extract for eight days, lost more than one-half of their cholinesterase activity on a milligram of protein basis, although the protein content of the cultured cells was maintained.
Addition of acetylcholine, acetyl β-methylcholine, and β-dimethyl aminoethyl acetate to the cultures maintained the total cholinesterase activity of the cultured cells compared with non-incubated cells, and prevented the decrease in enzyme activity per milligram of protein although the maintained level was lower than the original enzyme level. Propionyicholine and butyrylcholine were less effective than the above compounds in maintaining the enzyme level, and benzoylcholine and the "RC" analog of acetylcholine were ineffective in preventing the decrease in enzyme activity observed after 8 days incubation.
On the basis of a comparative study with 5 substrates, the cholinesterase of embryo chick intestine seemed to be neither the classical specific nor the nonspecific type of enzyme.
Footnotes
- Received February 1, 1957.
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