scispace - formally typeset
Search or ask a question

Showing papers on "Tartrate-resistant acid phosphatase published in 1982"


Journal ArticleDOI
TL;DR: Tartrate-resistant acid phosphatases of bone may be suitable biochemical probes for osteoclast function, but it will be necessary to achieve further purification in order to develop analytical methods with sufficient sensitivity and specificity to ensure precise localization and quantitation.
Abstract: Organ cultures of newborn mouse calvaria were used to test the hypothesis that tartrate-resistant acid phosphatase might serve as a biochemical marker for osteoclast function. When bone resorption was stimulated in vitro with either parathyroid hormone or 1,25(OH)2D3, there was a significant increase in both tartrate-resistant and tartrate-sensitivity acid phosphatase activity in the medium relative to cultured controls. Tartrate-resistant activity was localized histochemically primarily over the osteoclast and appeared as three distinct activity bands when electrophoresed on polyacrylamide gels. The tartrate-sensitive activity was found primarily associated with bone cells other than the osteoclast using histochemical techniques, and was resolved into five bands on polyacrylamide gels. The results obtained from biochemical assays, histochemical observations, and polyacrylamide gel electrophoresis suggest that bone resorption in vitro results in the release of tartrate-resistant acid phosphatase from osteoclasts and tartrate-sensitive acid phosphatase from other bone cells as well as osteoclasts. Tartrate-resistant acid phosphatases of bone may be suitable biochemical probes for osteoclasts function, but it will be necessary to achieve further purification in order to develop analytical methods with sufficient sensitivity and specificity (e.g., immunochemical) to ensure precise localization and quantitation.

961 citations


Journal ArticleDOI
K W Lam, M Siemens, T Sun, C Y Li, L T Yam 
TL;DR: An immunochemical method for quantitative analysis of the tartrate-resistant acid phosphatase (EC 3.3.1.2), band 5, is presented and is compared with previously described colorimetric and electrophoretic methods.
Abstract: An immunochemical method for quantitative analysis of the tartrate-resistant acid phosphatase (EC 3.1.3.2), band 5, is presented. This method involves precipitation of the enzyme from the serum by the antibody specific to band 5 and by sheep anti-rabbit immunoglobulin, followed by analysis of the enzyme activity in the precipitate. The precipitation procedure eliminates the interferences of the tartrate-sensitive phosphatase of all tissues, of the tartrate-resistant phosphatase of erythrocytes, and of unknown substances that interfere with the colorimetric method. We compare the present method with previously described colorimetric and electrophoretic methods.

37 citations



Journal ArticleDOI
TL;DR: It is indicated that T‐rAcP activity is observed not only in HCL cells but also in the well‐differentiated lymphoid cells such as ATL cells, B‐CLL and T-CLL cells except the most highly differentiated forms of B‐cells of MM and macroglobulinemia.
Abstract: Acid phosphatase (AcP) in neoplastic cells from various lymphoid leukemias was examined. In the cytochemical studies, tartrate-resistant AcP (T-rAcP) activity was observed in the neoplastic cells from well-differentiated lymphoid leukemias such as adult T-cell leukemia (ATL), B-cell chronic lymphocytic leukemia (B-CLL), T-cell chronic lymphocytic leukemia (T-CLL), and hairy-cell leukemia (HCL). T-rAcP activity was also detected in a small number of leukemic cells obtained from T-cell acute lymphoblastic leukemia (T-ALL), while it was not detected in the neoplastic cells from null-ALL, macroglobulinemia, and multiple myeloma (MM). In the electrophoretical studies, fraction 1 (F-1), F-3, F-3b, and F-4 were completely tartrate-sensitive, while F-2 was partially resistant and F-5 was completely resistant. T-rAcP activity (F-5) was observed in ATL cells, B-CLL cells, and HCL cells, while it was not detected in ALL cells, macroglobulinemia cells, and MM cells. The present study indicates that T-rAcP activity is observed not only in HCL cells but also in the well-differentiated lymphoid cells such as ATL cells, B-CLL and T-CLL cells except the most highly differentiated forms of B-cells of MM and macroglobulinemia.

13 citations