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Showing papers on "Tartrate-resistant acid phosphatase published in 1979"


Journal ArticleDOI
TL;DR: Acid phosphatase activity in homogenized tibiae and femora of suckling rats was extracted with 0.3M KCl and 0.1% Triton X-100 and E1 appears similar to the high molecular weight acid phosphatases of soft tissues, however, E2 appears to differ from the low molecular weightosphatases in soft tissues with regard to substrate specificity.
Abstract: Acid phosphatase activity in homogenized tibiae and femora of suckling rats was extracted with 0.3M KCl and 0.1% Triton X-100. A high-speed supernatant was treated with protamine sulfate, dialyzed, and chromatographed on CM-52 cellulose. All of the acid phosphatase activity was eluted with a sodium acetate buffer and combined ionic strength-pH gradient into two peaks (E1 and E2). Both enzyme peaks were further purified with Sephadex G-200, which resulted in 700- and 1000-fold purification for E2 and E1, respectively. A total of 220 units (µmoles substrate/min) of E2 with a specific activity of 160 units/mg protein has been obtained in one run by this procedure. E1 has a high molecular weight (>100,000) and shows preference for monophosphate ester substrates, is markedly inhibited by tartrate, and has a pH optimum near 5. E2 has a lower molecular weight (<40,000) and shows negligible activity with monophosphate esters [except withp-nitrophenyl phosphate (p-NPP)], but high activity with ADP and ATP. E2 is unaffected by tartrate and shows a pH optimum near 6. Both enzymes are competitively inhibited by inorganic phosphate, and E2, but not E1, is markedly inhibited byp-chloromercuribenzoate. Withp-NPP as substrate, E1 and E2 have distinctly different values for Km. E1 appears similar to the high molecular weight acid phosphatases of soft tissues. However, E2 appears to differ from the low molecular weight phosphatases in soft tissues with regard to substrate specificity.

45 citations



Journal ArticleDOI
TL;DR: Enzymatic cytochemical studies for acid phosphatase with and without tartrate may be helpful in the differential diagnosis of cutaneous T-cell lymphomas from variants of chronic dermatitis.
Abstract: Tartrate-resistant acid phosphatase has been known to be of diagnostic value in hairy cell leukemia. However, occasionally neoplastic cells of other varieties of lymphoproliferative disorders may contain tartrate-resistant acid phosphatase. The authors have studied four patients with Sezary syndrome who had typical cutaneous lesions with extensive lymphoid infiltrates and circulating atypical E-rosetting lymphoid cells. The abnormal Sezary cells accounted for 23-69% of the peripheral mononuclear cells and often showed convoluted or folded nuclei. These cells in all four patients were strongly positive for acid phosphatase resistant to tartaric acid inhibition. Enzymatic cytochemical studies for acid phosphatase with and without tartrate may be helpful in the differential diagnosis of cutaneous T-cell lymphomas from variants of chronic dermatitis.

17 citations