Pholas dactylus

Fig. 6.2.1 Diagram showing the luminous areas of the clams Pholas dactylus (top from Panceri, 1872) and Rocellaria grandis (bottom from Haneda, 1939).

Dubois, R. (1887). Fonction photogenique chez le Pholas dactylus. Compt. Rend. Soc. Biol. 39 564-566. 

Dunstan, S. L., et al. (2000). Cloning and expression of the bioluminescent photoprotein pholasin from the bivalve mollusc Pholas dactylus. J. Biol. Chem. 275 9403-9409. 

Henry, J. P., and Michelson, A. M. (1970). Studies in bioluminescence. IV. Properties of luciferin from Pholas dactylus. Biochim. Biophys. Acta 205 451-458. 

Henry, J. P., and Monny, C. (1977). Protein-protein interaction in the Pholas dactylus system of bioluminescence. Biochemistry 16 2517-2525. 

Michelson, A. M. (1978). Purification and properties of Pholas dactylus luciferin and luciferase. Method. Enzymol. 57 385-406. 

Pholasin is the protein-bound luciferin from the bivalve mollusc Pholas dactylus. This substrate reacts with its luciferase and molecular oxygen to produce light. The photoprotein, commercially available, undergoes an oxidative... 

The luciferase isolated from the burrowing clam Pholas dactylus is essentially a peroxidase, which oxidizes a complex oiganic side chain on the surface of a luciferin. This enzyme has not been used in imunoassays however, the luciferin is a substrate for horseradish peroxidase, which produces a very sensitive assay for that enzyme (38). 

L14. Longeon, A, Henry, J. P., and Henry, R., A solid-phase luminescent immunoassay for human chorionic gonadotrophin using Pholas dactylus bioluminescence. J. Immunol. Methods 89, 103-109 (1986). 

Luciferase (Pholas dactylus) =11 % carbohydrate content 0.707 (TJ 75H2... 

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