Showing papers on "Tartrate-resistant acid phosphatase published in 1985"

Tartrate-resistant acid phosphatase of human lung: apparent identity with osteoclastic acid phosphatase.

Abstract: Extracts of human lung tissue contain appreciable activities of a tartrate-resistant acid phosphatase which is apparently identical with the analogous enzyme in bone extracts, with respect to electrophoretic mobility, apparent molecular weight (ca. 37,000), Michaelis constants and relative rates of hydrolysis of various substrates. The acid phosphatase appears to be a constituent of alveolar macrophages. Lung provides a convenient source for the preparation of tartrate-resistant acid phosphatase.

Tartrate-resistant acid phosphatase in human alveolar macrophages.

Abstract: Tartrate-resistant acid phosphatase has been extracted from human alveolar macrophages, in which its specific activity is 10-fold that in whole lung. The apparent identity of the alveolar macrophage isoenzyme with that associated with osteoclasts suggests that both types of cell belong to the mononuclear phagocyte system. Within this system, expression of tartrate-resistant acid phosphatase appears to accompany certain kinds of differentiation.

Immunological characterization of human acid phosphatase gene products.

Abstract: The immunological cross-reactivity of heterogeneous acid phosphatase isozymes from different human tissues has been studied using monospecific antisera prepared against four homogeneous acid phosphatases. The enzyme characterized as tartrate-inhibitable, prostatic acid phosphatase is also found to be present in leukocytes, kidney, spleen, and placenta. The tartrate-inhibitable (liver) lysosomal enzyme is also found in kidney, fibroblasts, brain, placenta, and spleen, but it is not detectable in erythrocytes and prostate. In several tissues, 10-20% of the tartrate-inhibitable enzyme is not precipitated by any of the antisera used; an exceptionally high amount (54%) of such an enzyme is present in human brain. Antiserum against a low molecular weight tartrate-resistant liver enzyme (14 kDa) does not crossreact with the erythrocyte enzyme. (10-20 kDa). All other tissues except placenta, prostate, and fibroblast cells show a cross-reactivity with the 14-kDa acid phosphatase antiserum. Thus, the low molecular weight human liver acid phosphatase is distinct from the erythrocyte enzyme, and there are also at least three different tartrate-inhibitable acid phosphatases in human tissues. Chromosomal assignments have been made for only two of the (at least) five acid phosphatases that are present in adult human tissues.

Tartrate‐resistant acid phosphatase staining of monocytes in gaucher disease

Abstract: Cytochemical studies were performed on peripheral blood from 30 patients with type 1 Gaucher disease In 29 of the patients, peripheral blood monocytes stained positively for tartrate-resistant acid phosphatase, whereas monocytes from 18 normal individuals and 14 patients with monocytosis did not In the Gaucher patients, the percentage of monocyte positivity for tartrate-resistant acid phosphatase ranged from 2 to 97 There was no correlation between the percent monocyte staining and the degree of disease severity, as measured by hepatosplenomegaly, pancytopenia, or extent of bone disease, for the group as a whole In Gaucher patients who had not undergone splenectomy, however, there was a significant correlation between percent monocyte staining and the degree of hepatosplenomegaly, anemia, and thrombocytopenia The presence of tartrate-resistant acid phosphatase may be secondary to the lysosomal accumulation of glucosyl ceramide within these monocytes, although this remains to be confirmed If so, these circulating cells may represent precursors of the Gaucher cells in tissues Tartrate-resistant acid phosphatase staining of peripheral blood monocytes may be useful as a diagnostic marker for Gaucher type 1 disease and for further studies on the pathogenesis of the disease

Characterization of Fe2+-activated acid phosphatase in rat epidermis

Abstract: A particulate acid phosphatase (EC 3.1.3.2, orthophosphoric monoester phosphohydrolase (acid optimum)) was extracted in 1 M KCl, from 2-day rat epidermis. The enzyme has a Mr of 32,000, but two forms, F1 and F2 with pI values of 8.6 and 8.3, respectively, were identified while the pI values of other acid phosphatases soluble in sucrose and Triton X-100 were all acidic. F1 and F2 also differed from other epidermal acid phosphatases because they were (a) activated by Fe2+ and reducing agents, (b) showed immunological cross-reactivity with purple acid phosphatase of rat spleen and (c) dephosphorylated phosvitin and alpha-casein even though they had rather high Km values.

Isolation and characterization of a homogeneous acid phosphatase from catfish liver

Abstract: 1. 1. A homogeneous, tartrate-inhibitable acid phosphatase (AcPase) was obtained from the liver of channel catfish ( Ictalurus punctatus ) by the use of Affi Gel-10-coupled aminohexyltartramic acid affinity chromatography. 2. 2. The enzyme has a molecular weight of 82,500 and is a dimer consisting of two apparently equivalent subunits with subunit weights of 35,000 ± 3000. Amino acid composition data are presented and compared with those of mammalian acid phosphatases. 3. 3. Data suggest that the enzyme is a metalloacid phosphatase. 4. 4. Catfish liver AcPase exhibits two molecular forms with pI 5.66 and 5.37 which were separated by chromatofocusing. 5. 5. A spontaneous conversion of the less acidic form to a more acidic form was observed and this conversion was accompanied by a decreased sensitivity towards tartrate inhibition.