HISTOCHEMICAL STUDY OF A FLUORIDE RESISTANT ACID PHOSPHATASE REACTION IN THE MOUSE DUODENUM
- 1 March 1957
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 5 (2) , 135-139
- https://doi.org/10.1177/5.2.135
Abstract
A fluoride resistant acid phosphatase reaction (pH 5.0) has been demonstrated histochemically in the cuticular border of the mouse duodenum. This reaction was shown to be inactivated by the metal chelating agent, ethylene diamine tetraacetic acid, and reactivated by the following metallic salts : calcium chloride, cobalt(ous) nitrate, cupric sulfate, ferric chloride, ferric ammonium sulfate, ferrous sulfate, lead nitrate, lithium sulfate, magnesium sulfate, mercuric chloride, manganous chloride and zinc acetate. The two ferric salts produced the greatest amount of reactivation and cupric sulfate and manganous chloride produced the least amount of reactivation. These characteristics of inactivation by a metal chelating agent and metal reactivation plus the fluoride resistance of the acid phosphatase reaction present in the cuticular border of the mouse duodenum are features more typical of an alkaline type of phosphatase rather than the acid variety. This suggests that alkaline type phosphatase may be demonstrable histochemically in the cuticular border of the mouse duodenum in the acid pH range.Keywords
This publication has 6 references indexed in Scilit:
- Quantitative studies of beta-glycerophosphatase activity in normal and neoplastic tissuesCancer, 1956
- THE HISTOCHEMICAL DEMONSTRATION OF ACID PHOSPHATASE BY A POST-INCUBATION COUPLING TECHNIQUEJournal of Histochemistry & Cytochemistry, 1955
- Use of an Organic Chelating Agent in Histochemical Study of Alkaline Phosphatase Activation.Experimental Biology and Medicine, 1953
- ROLE OF METAL IONS IN ENZYME SYSTEMSPhysiological Reviews, 1950
- Properties of the acid phosphatases of erythrocytes and of the human prostate glandBiochemical Journal, 1949
- The cytological localization, substrate specificity, and pH optima of phosphatases in the duodenum of the mouseJournal of Cellular and Comparative Physiology, 1946