Histochemical demonstration of non-specific esterases and non-specific acid phosphatases using menadiol substrates.

Although many synthetic substrates and methods are available for the histochemical detection of non-specific esterases and non-specific acid phosphatase, there are still further possibilities to investigate these hydrolases histochemically. This was shown for menadiol diacetate and menadiol diphosphate using tetrazolium salt, simultaneous azo-dye as well as metal salt methods in many rat tissues. In comparison, the azo-dye procedure with various Fast salts or hexazonium Pararosaniline or New Fuchsin delivered less satisfactory results; precisely localized stain in sufficient amounts was obtained for non-specific esterases using nitro BT, tetranitro BT or benzothiazolystyrylphthalhydrazidyl tetrazolium (BSPT) and for non-specific acid phosphatase with BSPT in the tetrazolium salt method or using cerium ions for phosphate trapping in the diaminobenzidine-nickel-hydrogen peroxide procedure.

Menadiol diphosphate, a new substrate for non-specific alkaline phosphatase in histochemistry and immunohistochemistry.

Menadiol diphosphate was introduced as a new substrate for nonspecific alkaline phosphatase, following a search for new and less expensive substrates, which give a more sensitive response and are easily synthesized in the laboratory. Menadiol released by phosphatase action can be assayed by its reduction of tetrazolium salts, or it can be coupled with diazonium salts; alternatively, the phosphate can be trapped by metal ions. The synthesis and purification of menadiol diphosphate are described, and it was shown to be sufficiently stable for qualitative and semiquantitative histochemistry, as well as for the immunohistochemistry of enzymes and cytoskeletal proteins with nonspecific alkaline phosphatase as the enzyme label.

[Alkaline phosphatase in human lymphocytes. II. A method for ultracytochemical detection of alkaline phosphatase in lymphocytes].

For the ultracytochemical identification of alkaline phosphatase in lymphocytes gained from the peripheral blood of healthy individuals a sensitive method is described which allows the low enzyme activity of these cells to be determined. This was possible because the authors succeeded in stabilizing lead ions in the alkaline medium by forming a complex directly between tris-(hydroxymethyl) aminomethan and lead (II) citrate. AP localized ultrachemically in lymphocytes in particular formations similar to phosphasomes of neutrophilic granulocytes.

[Alkaline phosphatase in human lymphocytes. I. Cytochemical detection of alkaline phosphatase in normal human peripheral blood lymphocytes].

The present paper deals with a sensitive cytochemical method of identifying alkaline phosphatase (AP) in rosette-forming lymphocytes gained from the peripheral blood of healthy human beings. The percentage of AP-positive lymphocytes amounts to 5%, with all cells comprising B- and O-lymphocyte population and with T-lymphocytes being negative. In a group of healthy test persons, recently, however, having undergone various inflammatory processes or virus diseases, the number of AP-positive lymphocytes is significantly higher, from 41-73% in B- and O-lymphocytes and from 6-38% in T-lymphocytes.

[Histochemical evidence of aminotransferases. VII. Quantitative histochemical and biochemical investigations of the amino-transferases of branched chain amino acids, glycine and serine in the rat organs during development (author's transl)].

Ontogenetic changes of the activity and isoenzymes of the aminotransferases of branched chain amino acids, glycine and serine in the rat organs have been studied by quantitative histochemical method and by electrophoresis. An increase of the enzymatic activity with the 3 branched chain amino acids has been observed up to the 7th day after birth. Thereafter the changes with leucine and isoleucine are rather similar.