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Showing papers on "Tartrate-resistant acid phosphatase published in 1978"


Journal ArticleDOI
TL;DR: The naphthol--ASBI phosphoric acid--fast garnet GBC method is sensitive, technically simple and easily reproducible, and its reaction product is highly chromogenic and is most suitable for cytochemical demonstration of acid phosphatase and tartrate-resistant acid phosphate activity in cytologic preparations.
Abstract: Cytochemical demonstration of tartrate-resistant acid phosphatase activity is essential for the diagnosis of leukemic reticuloendotheliosis. In order to perform this test correctly and to interpret the results propertly, it is necessary to understand the technical details of the cytochemical methods thoroughly. The method using naphthol--ASBI phosphoric acid--fast garnet GBC is recommended for this purpose, and factors crucial to the cytochemical study, such as fixation, substrate, coupler, pH and temperature of incubation buffer, counterstains, and mounting media are examined and discussed. Conventional methods for acid phosphatase in the presence and absence of L(+) tartaric acid are also critically examined. The naphthol--ASBI phosphoric acid--fast garnet GBC method is sensitive, technically simple and easily reproducible. Its reaction product is highly chromogenic and is most suitable for cytochemical demonstration of acid phosphatase and tartrate-resistant acid phosphatase activity in cytologic preparations. The naphthol--ASBI phosphoric acid--pararosaniline method is highly specific and is best for histochemical demonstration of acid phosphatase and tartrate-resistant acid phosphatase in tissue sections.

110 citations


Journal ArticleDOI
TL;DR: The major acid phosphatase in children's sera is shown to be an acid pyrophosphatase, band 5b, which is indistinguishable from the enzyme previously isolated from the spleen of leukemic reticuloendotheliosis.
Abstract: Spectrophotometry of total acid phosphatase activity in children's sera showed an average value of 22.4 +/- 2.9 and 7.4 +/- 0.8 U/liter, for the hydrolysis of p-nitrophenyl phosphate and alpha-naphthyl phosphate, respectively. Analyses of "band 5b", after electrophoresis on acrylamide gel, gave even higher values. The values for children's sera were much higher than those for sera from adults. The multiplicity of acid phosphatases in sera of children and adults was studied by electrophoresis on acrylamide gel and by chromatography on CM-Sepharose. Both methods showed the major acid phosphatase in children's sera to be an acid pyrophosphatase, band 5b. Its catalytic properties are indistinguishable from the enzyme previously isolated from the spleen of leukemic reticuloendotheliosis.

84 citations


Journal ArticleDOI
TL;DR: The cytochemical results underline that prolymphocytic leukemia indeed is a separate entity which can be differentiated from hairy cell leukemia and chronic lymphatic leukemia not only morphologically but also cytochemically.
Abstract: In a typical case of prolymphocytic leukemia, blood smears and lymph node imprints have been investigated cytologically and cytochemically It could be shown that many leukemic cells in both blood smears and lymph node imprints contained tartrate resistant acid phosphatase activity Furthermore, the lymph node imprints disclosed many cells with a positive alkaline phosphatase reaction Such a reaction hitherto has not been described in malignant cells of lymphoproliferative diseases The cytochemical results underline that prolymphocytic leukemia indeed is a separate entity which can be differentiated from hairy cell leukemia and chronic lymphatic leukemia not only morphologically but also cytochemically In addition, the case shows that leukemic blood cells are not inevitably identical with those occurring in organ infiltrates

10 citations



Journal ArticleDOI
TL;DR: Acid phosphatase of newborn rat epidermis was purified about 270‐fold by a procedure including acid treatment, CM‐cellulose, DEAE‐ cellulose chromatography, and gel filtration on Sephadex G‐100.
Abstract: Acid phosphatase of newborn rat epidermis was purified about 270-fold by a procedure including acid treatment, CM-cellulose, DEAE-cellulose chromatography, and gel filtration on Sephadex G-100. The purified enzyme had a pH optimum of 5.0 and an optimal temperature of 40°C. The enzyme was not activated by divalent cations, ethylenediaminetetraacetic acid or 2-mercaptoethanol, and it was inhibited by p-chloromercuribenzoate. The inhibition pattern by fluoride and by L(+) tartrate was competitive. The Km value for p-nitrophenyl phosphate was 3.84×10−5 M, and the molecular weight was about 73, 000. The enzyme appeared to be a nonspecific acid phosphatase. Intracellular localization of acid phosphatase in the epidermis was discussed.