Acid Phosphatase in Clonorchis sinensis
- 1 April 1964
- journal article
- research article
- Published by JSTOR in Journal of Parasitology
- Vol. 50 (2) , 235-+
- https://doi.org/10.2307/3276276
Abstract
Evidence is presented that the level of acid phosphatase is high in the tissue of Clonorchis sinensis. The properties of the enzyme were studied by (1) various chemical substances that inhibit or activate enzyme activity, (2) pH -activity curves, and (3) starch gel electrophoresis. The pH -activity curves revealed three peaks at pH 4.0, 4.5, and 5.5. The enzyme was separated electrophoretically into three fractions, with different Michaelis constants. The results suggest the presence of acid phosphatase isozymes in the parasite. This enzyme was found to be distributed all over the body surface. Alkaline phosphatase was found to be low in the tissue of the parasite.Keywords
This publication has 13 references indexed in Scilit:
- Molecular Heterogeneity and Evolution of EnzymesScience, 1960
- Histochemical Observations of Alkaline Phosphatase in Schistosoma MansoniThe Journal of Infectious Diseases, 1959
- Studies on alkaline phosphatases. 1. Kinetics of plasma phosphatase of normal and rachitic chicksBiochemical Journal, 1959
- MULTIPLE FORMS OF ENZYMES: TISSUE, ONTOGENETIC, AND SPECIES SPECIFIC PATTERNSProceedings of the National Academy of Sciences, 1959
- The acid phosphatases of rat liverBiochemical Journal, 1957
- Acid phosphatase. V. The nature of inactivation and stabilization of purified human red cell phosphomonoesteraseArchives of Biochemistry and Biophysics, 1955
- Acid phosphatase. III. Specific kinetic properties of highly purified human prostatic phosphomonoesteraseArchives of Biochemistry and Biophysics, 1955
- Acid phosphatase. II. Purification of human red cell phosphomonoesteraseArchives of Biochemistry and Biophysics, 1954
- Studies on the purification of acid prostatic phosphataseArchives of Biochemistry and Biophysics, 1953
- Properties of the acid phosphatases of erythrocytes and of the human prostate glandBiochemical Journal, 1949