LOCALIZATION AND MULTIPLE FORMS OF ACETYLCHOLINESTERASE IN SEA URCHIN EMBRYOS

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Abstract
Acetylcholinesterase during the development of the sea urchin Pseudocentrotus depressus was examined by enzyme assay (the colorimetric method of Ellmanet al.), histochemistry (a Cu-thiocholine method), polyacrylamide gel electrophoresis and DEAE-Sephadex ion exchange chromatography. The enzyme activity is detected in the unfertilized egg, remains low during cleavage, elevates slightly through gastrulation, and then increases rapidly thereafter. The intense activity is localized in the mesenchyme cells associated with the larval skeleton of young pluteus larvae, and their cell membranes and nuclear envelops. Soluble enzyme accounts for 60% of the total activity. The additional 34% is extracted by 1% Triton X-100 from particulates. The soluble enzyme consists of two forms. Both are strongly acidic proteins which are similar in electric charge, but dissimilar in size, being 180,000 and 280,000 in molecular weights. The enzyme released from the membrane by the detergent possesses a component which is not present in the soluble complement of the enzyme. It is not a secondary product of the soluble enzyme interacting with the detergent. Acetylcholinesterase serves as a marker of late differentiation and regional differentiation in the sea urchin embryo.