title: Cytochemical localization of acid phosphatase and trimetaphosphatase activities in Kurloff cells.
abstract: After stimulation of guinea pigs with estradiol to increase their Kurloff cell number, spleen imprints were prepared in order to detect non-specific acid phosphatase (AcPase) activity by light microscopic cytochemistry using naphthol AS-BI phosphate as substrate and pararosanilin or fast garnet GBC as coupler. For ultracytochemistry, Kurloff cells were prepared from spleens by filtration through a homogeneizer screen followed by repeated centrifugation. AcPase and trimetaphosphatase activities were tested using beta-glycerophosphate, cytidine-5'-monophosphate and inorganic trimetaphosphate as substrates. Significant enzymatic activities were demonstrated with all the substrates used in the cytoplasmic inclusion body of the Kurloff cells.
mesh_terms: D017766:Acid Anhydride Hydrolases; D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D004958:Estradiol / Q000494:pharmacology; D005260:Female; D006168:Guinea Pigs; D006651:Histocytochemistry; D008297:Male; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D013154:Spleen / Q000166:cytology / Q000187:drug effects / Q000201:enzymology*
chemical_list: D004958:Estradiol; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases; D017766:Acid Anhydride Hydrolases; C022768:trimetaphosphatase