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Title: Cytochemical localization of acid phosphatase and trimetaphosphatase activities in Kurloff cells. Author: Tiffon Y, Buat ML, Landemore G, Izard J. Journal: Biol Cell; 1986; 56(1):85-7. PubMed ID: 3013351. 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.[Abstract] [Full Text] [Related] [New Search]