The presence and isolation of a highly zinc activated acid phosphatase in the rat brain (author's transl)

The paper describes an acid phosphatase from rat brain extracts, which is highly activated by zinc acetate. The separation of the different acid phosphatases was performed by gel electrofocusing. After staining with 1-naphthyl phosphate and hexazonium pararosanilin or stabilized diazonium salts in t...

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Bibliographic Details
Published inActa histochemica Vol. 53; no. 2; p. 281
Main Authors Felicetti, D, Rath, F W
Format Journal Article
LanguageGerman
Published Germany 1975
Subjects
Acetates - pharmacology
Acid Phosphatase - analysis
Acid Phosphatase - isolation & purification
Animals
Brain - drug effects
Brain - enzymology
Choroid Plexus - enzymology
Chromatography, Gel
Histocytochemistry
Isoelectric Focusing
Male
Molecular Weight
Rats
Rats, Inbred Strains
Stimulation, Chemical
Zinc - pharmacology
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Summary:The paper describes an acid phosphatase from rat brain extracts, which is highly activated by zinc acetate. The separation of the different acid phosphatases was performed by gel electrofocusing. After staining with 1-naphthyl phosphate and hexazonium pararosanilin or stabilized diazonium salts in the presence of zinc acetate and sodium tartrate is this zinc activable enzyme fraction nearly selectively demonstrable. With the method of gelfiltration on Sephadex G 100 two fractions of acid phosphatase splitting 4-nitrophenyl phosphate with a very different molecular weight were obtained. In the presence of zinc acetate a third peak of acid phosphatase appears, which is highly activated by zinc and is different from the two other phosphatases. The gel electrofocusing of the last peak showed that it is identical with the above described, though not yet pure. By the fact that it can hydrolyze both 1-naphthyl phosphate and 4-nitrophenyl phosphate at pH = 4.8 and that it is activated by zinc acetate but resistant to tartrate, we would call it zinc activable tartrat resistant acid phosphatase. It is possible to demonstrate this enzyme histochemically. The enzyme activity is especially high in the stromal cells of the plexus chorioideus. After further purification and characterization of this enzyme it could be possible to distinguish it from other zinc activable acid phosphatases in different tissues and body fluids.
ISSN:0065-1281