Phosphatase localization in the endomembrane system of the dinoflagellate Crypthecodinium cohnii.
The distribution of four enzymes within the endomembrane system of the protist Crypthecodinium cohnii has been determined using cytochemical localizations with lead as a capture agent. Nucleoside diphosphatase (NDPase) activity, using inosine diphosphate (IDP) and thiamine pyrophosphate (TPP) as substrates, was observed in the Golgi apparatus, with a gradient of increasing reaction product noted in some cells from the cis to trans cisternae. Tubules and vesicles associated with the trans cisternae also contained reaction product. The endoplasmic reticulum exhibited a high activity of glucose-6-phosphatase [with glucose-6-phosphate (G-6-P) as substrate]. Traces of reaction product were also observed in the cis-most and trans-most cisternae of the dictyosomes. Activity of acid phosphatase (AcPase) was observed in Golgi cisternae as well as in associated cytoplasmic vesicles. Heaviest deposition was localized in medial and trans dictyosome cisternae. The cytoplasmic system of flattened vesicles subtending the surface membranes in these cells did not exhibit reactivity with any of the substrates used. The distribution of these enzymes in this algal cell appears similar to that observed in animal cells and suggests that these enzymes may represent markers for algal cell endomembrane compartments.
D017766:Acid Anhydride Hydrolases; D000135:Acid Phosphatase / Q000032:analysis; D004141:Dinoflagellida / Q000201:enzymology* / Q000648:ultrastructure; D004721:Endoplasmic Reticulum / Q000201:enzymology; D005952:Glucose-6-Phosphatase / Q000032:analysis; D006056:Golgi Apparatus / Q000201:enzymology; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D013834:Thiamine Pyrophosphatase / Q000032:analysis
D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases; D005952:Glucose-6-Phosphatase; D017766:Acid Anhydride Hydrolases; D013834:Thiamine Pyrophosphatase; C021446:inosine diphosphatase; C023837:nucleoside-diphosphatase