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histoplasmosis/phosphatase

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The pathognomonic "hairy cell" of leukemic reticuloendotheliosis was studied for ultrastructural localization of tartrate-resistant acid phosphatase activity. The enzyme activity could not be demonstrated by Gomori's method, but it was readily demonstrated in the cytoplasmic vesicles and Golgi
A fresh spleen sample obtained from a patient with leukemic reticuloendotheliosis was homogenized and subjected to centrifugation on a sucrose density gradient. A major portion of acid phosphatase band 5 was observed in the lysosome, confirming that the elevated phosphatase activity in the
A strong activity of the tartrate-resistant acid phosphatase, isoenzyme 5b, was observed in mouse spleen. The enzyme of the mouse spleen had similar electrophoretic mobility and related antigenicity to that of the reticulum cells of leukemic reticuloendotheliosis. Enzyme histochemical studies showed
The tartrate-resistant acid phosphatase was isolated from the spleen of a patient with leukemic reticuloendotheliosis. The unique characteristic of the enzyme is its similar reactivity toward p-nitrophenylphosphate, inorganic pyrophosphate ADP, and ATP. When ATP was incubated with the enzyme, the
A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as

Comparison of the tartrate-resistant acid phosphatase in Gaucher's disease and leukemic reticuloendotheliosis.

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Tartrate-resistant acid phosphatase was isolated from serum and spleen of patients affected by Gaucher's disease. Electrophoretic and antigenic properties were compared to the enzyme isolated from hairy cells described in a previous study (9). The enzyme isolated from Gaucher serum has

"Marching Cavity" of histoplasmosis in a patient with leukocyte alkaline phosphatase deficiency.

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Tartrate-resistant acid phosphatase isoenzyme in the reticulum cells of leukemic reticuloendotheliosis.

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Histochemical study of acid phosphatase isoenzyme in leukemic reticuloendotheliosis.

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We purified acid phosphatase isoenzyme 5b from a human spleen affected by leukemic reticuloendotheliosis and used it to produce a specific antiserum. The antiserum was used to show complete immunological identity among isoenzymes 5a and 5b in human serum, and 5b isolated from a giant-cell bone tumor

Progressive disseminated histoplasmosis; favorable response to ketoconazole.

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Four patients with disseminated histoplasmosis, two of whom had late relapses after previous therapy with amphotericin B, were treated with ketoconazole 200 to 400 mg daily for 1 year. All patients improved markedly during therapy, with resolution of symptoms decreasing liver and spleen size, and
Reticuloendotheliosis virus strain T (REV-T) is a highly oncogenic avian retrovirus which causes a rapid neoplastic disease of the lymphoreticular system. We derived six cell lines (1-3, 1-5, 2-10, 2-14, 2-16, and 2-20) from chicken spleen cells infected with REV-T. These cells can produce both the

Tartrate-resistant (band 5) acid phosphatase activity measured by electrophoresis on acrylamide gel.

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A tartrate-resistant acid phosphatase was isolated from a huma spleen infiltrated with reticulum cells of leukemic reticuloendotheliosis. The purified enzyme was used to establish the optimal conditions for quantitative analysis of this enzyme by electrophoresis on acrylamide gel. As little as 0.1

Malignant lymphoma simulating leukemic reticuloendotheliosis: a clinicopathologic study of ten cases.

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We have studied ten patients with a lymphoproliferative disorder characterized by massive splenomegaly; minimal lymphadenopathy; varying degrees of blood cytopenias; circulating atypical lymphoid cells frequently with "hairy" cytoplasm; monoclonal serum paraprotein; and tartrate-resistant acid
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