1966ParasitologyRequires access

Physiological studies on trematodes: phosphatase systems inGastrothylax crumenifer

Madan M. Goil

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Abstract

Biochemical studies on the phosphatase systems ofGastrothylax crumeniferhave been made. The maximum activity of the phosphatase enzyme was found to be at 5 pH. The action of magnesium and fluoride ions on the acid phosphatase activity shows that both act as inhibitors. The day-to-day variation in the phosphatase activity of the samples, as measured by block differences, was found to be significant at different pH levels. The heat denatured extract showed low and fairly constant acid phosphatase activity.

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What this paper is about

Biochemical studies on the phosphatase systems ofGastrothylax crumeniferhave been made. The maximum activity of the phosphatase enzyme was found to be at 5 pH. The action of magnesium and fluoride ions on the acid phosphatase activity shows that both act as inhibitors. The day-to-day variation in the phosphatase activity of the samples, as measured by block differences, was found to be significant at different pH levels. The heat denatured extract showed low and fairly constant acid phosphatase activity.

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Available abstract

Biochemical studies on the phosphatase systems ofGastrothylax crumeniferhave been made. The maximum activity of the phosphatase enzyme was found to be at 5 pH. The action of magnesium and fluoride ions on the acid phosphatase activity shows that both act as inhibitors. The day-to-day variation in the phosphatase activity of the samples, as measured by block differences, was found to be significant at different pH levels. The heat denatured extract showed low and fairly constant acid phosphatase activity.

Key concepts: Acid phosphatase, Phosphatase, Biology, Alkaline phosphatase, Enzyme, Biochemistry, Enzyme assay, Fluoride

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