Studies on Leukocyte Phosphatases. III. Inhibition of Leukocyte Acid Phosphatase by Zinc

1971 ◽  
Vol 17 (12) ◽  
pp. 1176-1179 ◽  
Author(s):  
Lawrence R DeChatelet ◽  
M Robert Cooper ◽  
Charles E McCall

Abstract Whereas the activity of leukocyte alkaline phosphatase is stimulated by Zn2+, it inhibits acid phosphatase activity. The degree of inhibition of acid phosphatase depends on the pH of the medium, being greater as the pH approaches neutrality. This inhibition may be at least partially reversed by the addition of amino acids, which suggests that interactions of Zn2+ and amino acids may play an important role in regulating the overall phosphatase activity of the leukocyte.

1970 ◽  
Vol 16 (9) ◽  
pp. 798-799 ◽  
Author(s):  
Lawrence R DeChatelet ◽  
M Robert Cooper ◽  
Charles E McCall

Abstract Leukocyte phosphatase activity was determined over a broad pH range. Using this procedure, we found no alkaline phosphatase activity in leukocytes from three patients with chronic granulocytic leukemia. The low values usually reported for this disease are actually attributable to acid phosphatase activity, which is slight but measurable at alkaline pH.


1989 ◽  
Vol 67 (3) ◽  
pp. 750-753 ◽  
Author(s):  
Iwan Ho

Seventeen isolates, encompassing five genera and eight species of ectomycorrhizal fungi, were compared for acid phosphatase, alkaline phosphatase, and nitrate reductase activity. Isolates within species differed in enzyme activity and isozyme patterns by host specificity and site (as exemplified by the genus Suillus). Host and site may have affected phosphatase enzyme activity. Generally, the Douglas-fir associates, which dominate in mesic sites, have higher acid phosphatase activity than pine associates, which mostly occupy xeric sites; however, pine associates from mesic sites also have higher acid phosphatase activity (e.g., S. tomentosus). In four isolates of Amanita muscaria, the effect of site was also apparent. Two of them, which have significantly higher acid phosphatase activity than the others, were isolated from mesic sites. The isozyme pattern of the genus Suillus appeared to be separated by host groups. Other isolates with only one species also differed more or less by host groups. They shared at least one band within host groups, except for the two isolates of Paxillus involutus from different hosts. The P. involutus S-403 isolated from an orchard showed much higher nitrate reductase activity than all other isolates. No apparent differences in nitrate reductase activity were found between the other isolates.


2020 ◽  
Vol 66 (No. 2) ◽  
pp. 93-98
Author(s):  
Beata Kuziemska ◽  
Andrzej Wysokiński ◽  
Joanna Trębicka

A three-year pot experiment carried out in the vegetation hall in 2014–2016 included studying the enzymatic activity of soil, into which various amounts of copper: (100, 200 and 300 mg Cu/kg soil) and organic materials (cattle manure, chicken manure, post-mushroom substrate) were introduced, used separately, at a soil-introduction dose of 2 g C<sub>org</sub>/kg. Copper and organic materials were used once, only in the first year of the study, before sowing test plant orchard grass. In soil collected after the last (fourth) swath of grass in each year of the study, the activity of urease, dehydrogenases, acid, and alkaline phosphatase was determined. Applications of copper to the soil, regardless of its dose, resulted in a decrease in urease, dehydrogenases and alkaline phosphatase and an increase in acid phosphatase activity. The inactivating effect of this metal on the activity of urease, dehydrogenases and alkaline phosphatase increased with the increase of its dose. Organic fertilisation generally increased the enzymatic activity of the analysed soil. In subsequent years of the study, urease and alkaline phosphatase activity decreased, while acid phosphatase activity increased. Dehydrogenase activity did not change significantly in subsequent years of the study.  


Author(s):  
Ragnar Fänge

Activities of phosphomonoesterases were measured at acid and at alkaline reaction (pH 4–5 or 9–65) in homogenates of elasmobranch tissues especially lymphomyeloid structures. The animals were dogfish (Scyliorhinus caniculd) and two species of ray (Raja brachyura, R. naevus). Acid phosphatase activity was high in the epigonal tissue, Leydig's organ, the spleen and the thymus. High activity was also found in the pancreas and the kidney, whereas skeletal and cardiac muscle showed low values. The activity of alkaline phosphatase was very high in the kidney and relatively low in other tissues. Ultrasonification of homogenates from the dogfish resulted in increase of acid phosphatase activity but had little effect on alkaline phosphatase activity. The high activity of acid phosphatase in lymphomyeloid tissue may be due to the presence of large numbers of various types of leucocytes.


1959 ◽  
Vol 7 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M. S. BURSTONE

High acid phosphatase activity was observed in osteoclasts of several species using a reproducible azo-dye technique. High activity of two distinct enzymes, acid and alkaline phosphatase, are associated with osteoclasts and osteoblasts respectivey. Althouth frozen-dried tissues are recommended for definitive studies, the enzyme techniques used give satisfactory results with cold acetone-fixed tissues. The most accurate localization of acid phosphatase in osteoclasts in controlled comparative studies is obtained with double-embedded frozen-dried undecalcified tissues in conjunction with naphthol AS-phosphates.


1971 ◽  
Vol 17 (3) ◽  
pp. 210-213 ◽  
Author(s):  
Lawrence R DeChatelet ◽  
James V Volk ◽  
Charles E McCall ◽  
M Robert Cooper

Abstract The activity of leukocyte alkaline phosphatase is inhibited by a number of amino acids, most notably cysteine and histidine. The mechanism of this inhibition involves chelation of Zn2+ by the amino acids, as indicated by the complete reversal of the inhibition by added Zn2+. The concentrations of amino acids and Zn2+ required to affect the enzyme activity are such that their interaction might represent an in vivo mechanism for the control of leukocyte alkaline phosphatase activity.


2000 ◽  
Vol 80 (1) ◽  
pp. 91-97 ◽  
Author(s):  
B. Gagnon ◽  
R. Lalande ◽  
R. R. Simard ◽  
M. Roy

Combined primary and secondary papermill sludge (PS) is a good source of C and other nutrients for soils devoted to intensive horticultural production. A field study was conducted to evaluate the effect of PS, spring-applied alone or in combination with ammonium nitrate (AN), on the enzymatic activity of a Bedford clay (Humic Gleysol) in the province of Québec, Canada. The experiment was started in 1996 with winter cabbage (Brassica oleracea var. capitata L.) and continued in 1997 and 1998 on the same plots with sweet corn (Zea mays L.). The PS was applied at 0 (control), 8, 16, 32 and 65 Mg ha−1 in 1996 and at 44% of these rates in 1997. No sludge was applied in 1998. Additional treatments consisted of AN applied yearly at 100% of the plant N requirements and a PS and AN combination. Soil arylsulfatase and acid and alkaline phosphatase activities were measured at three different times in each growing season. The PS rate linearly increased the soil acid phosphatase activity in all 3 yr. In contrast, the alkaline phosphatase and arylsulfatase activities were enhanced in 1997 by the 8–16 Mg PS ha−1 treatments, whereas larger amounts of PS showed activity comparable to the control. The second PS application promoted phosphatase activities mostly in fall, but did not sustain arylsulfatase activity. The AN gave lower phosphatase activities than PS, and depressed arylsulfatase. Addition of AN to PS increased only acid phosphatase activity as compared with PS alone or the control. This study indicated that addition of PS improved enzyme activity of this horticultural soil but rates in excess to 32 Mg ha−1 may be detrimental. Key words: Papermill sludge, soil enzyme, cabbage, corn


1968 ◽  
Vol 100 (6) ◽  
pp. 649-655 ◽  
Author(s):  
S. N. H. Naqvi ◽  
Shahid H. Ashrafi ◽  
M. A. H. Qadri

AbstractThe acid and alkaline phosphatase activity was measured in the developing egg and in the alimentary canal of aging nymphs as well as adult males and females of different ages. Para-nitrophenol was used as colorimetric standard and disodium p-nitrophenyl phosphate as substrate. Activity was measured in terms of micromoles of p-nitrophenol liberated from the substrate as a result of enzyme action.Acid phosphatase activity was noticed to increase with the embryonic development and was higher than in the case of alkaline phosphatase. The alkaline phosphatase activity was lowest in the freshly laid egg, but increased more sharply than acid phosphatase during embryonic development.The activity of both the acid and alkaline phosphatases was highest in the first instar and declined gradually to the fifth instar. The activity of acid phosphatase was higher than alkaline phosphatase in all stages except the first instar where it was almost equal. The activity of both the enzymes was higher during the intermoulting period and declined at each moult indicating a hormone–enzyme relationship.In adults, activity of both the enzymes increased up to the maturation period after which the activity gradually decreased. Acid phosphatase activity was generally higher in males whereas alkaline phosphatase activity was generally higher in females. In almost all cases, the acid phosphatase activity was found to be higher than the alkaline phosphatase.


1967 ◽  
Vol 15 (6) ◽  
pp. 311-334 ◽  
Author(s):  
B. K. WETZEL ◽  
S. S. SPICER ◽  
R. G. HORN

In rabbit heterophils, acid phosphatase activity occurs in primary (azurophil) granules which predominate in early cells and persist in mature cells and in tertiary granules which are seen only in mature cells. Alkaline phosphatase activity occurs in secondary granules which appear in intermediate heterophils and later predominate in mature cells. Acid phosphatase activity in heterophil Golgi zones coincides developmentally with the genesis of primary and, later, tertiary granules, whereas alkaline phosphatase in the Golgi complex coincides with secondary granulogenesis. In developing eosinophils, acid phosphatase reaction product occurs in Golgi elements, rims the spherical precursors of angular, mature granules and appears inconsistently within mature granules. Basophil myelocytes show acid phosphatase in Golgi elements but not in specific granules. Additional acid phosphatase reactive structures include: granules of mononuclear cells; phagocytic vacuoles in macrophages; autophagic vacuoles in maturing erythroid cells; small dense granules of platelets; dense bodies in lipocytes; and Golgi elements of mononuclear cells, macrophages, nucleated red cells, megakaryocytes and lipocytes. Localized deposits were absent in control specimens except for enzyme-independent nuclear staining in alkaline phosphatase preparations.


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