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Aspartate trans carbamylase of the scallop pecten maximus mollusca lamellibranchia method of assay and variations in the activity in mantle and gonad


Aspartate trans carbamylase of the scallop pecten maximus mollusca lamellibranchia method of assay and variations in the activity in mantle and gonad



Journal of Experimental Marine Biology and Ecology 50(1): 99-117



ISSN/ISBN: 0022-0981

The experiments to test the value of an index for estimate of the in situ growth rate of marine animals were carried out on the scallop P. maximus L. At 35.degree. C the scallop ATC [aspartate transcarbamylase] shows an optimum pH of 9 and a Km of 4.6 .times. 10-3 M for aspartate and of 8.0 .times. 10-4 M for carbamyl phosphate. The different types of inhibition by the substrates' high concentrations and the products suggest an ordered sequential mechanism for the reaction. The decrease in enzyme activity due to metallic ions (Cu2+ and Zn2+) and to p-hydroxymercuribenzoate is compatible with the presence of a sulfhydryl group in the active site. The variations in ATC levels within the gonad and mantle of the scallop were measured and compared with the sexual maturation and somatic growth in a natural population. A correlation between the ATC specific activity and the relative growth rate is demonstrated.

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Accession: 004783272

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