Acid Phosphatase Activity

Measurement of serum acid phosphatase activities as an aid in the diagnosis and treatment of advanced prostatic carcinoma is based on the observation by Gutman and Gutman that the activity is elevated by skeletal metastases ( ). Many workers have... 

Nodular hyperplasia of the prostate is usually associated with a normal serum acid phosphatase activity. Complications such as acute urinary obstruction or prostatic infarction will elevate this serum activity for several days as will cystoscopy and catheterization (98). Digital palpation of the prostate may result in an elevation which subsides within a few hours. 

Bioassay for metabolic activity (glycolytic and acid phosphatase activity) of peritoneal-exudative cells after treatment with polysaccharide practions. 

B. Dindelaker and H. Marschner, In vivo demonstration of acid phosphatase activity in the rhizosphere of soil-grown plants. Plant Soil 144 99 (1992). 

Decreases in sperm motility and increased acid phosphatase activity were reported to result from oral administration of 0.05 mg/kg lead in drinking water to male rats for 20-30 days in a study from the former U.S.S.R. (Krasovskii et al. 1979). Dystrophic changes of the Leydig cells were reported in gonadal tissues of rats exposed to doses as low as 0.005 mg lead/kg/day. The weaknesses of the study include absence of data on the strain and number of rats used, and the fact that PbB levels were not reported. 

Associated with NA depletion from host nuclei was the diminution and deformation of these nuclei, significant depletion of host nucleoskeletal protein lamin b, and significant reductions in levels of host cell RNA, protein and acid phosphatase activity. In contrast, host infiltrating cells showed no such changes, supporting an infected cell-specific effect. These observations support the possibility that NA are synthesized by the parasite and modulate host nuclear functions. However, release of other parasite secretory products, not analysed, might have been inhibited in these experiments also. 

Hyperproteinemia, hyperglycemia, and enhanced serum alkaline and acid phosphatase activities (WHO 1984)... 

Chau Y-P, Lu K-S. ZIO impregnation and cytochemical localization of thiamine pyrophosphatase and acid phosphatase activities in small granule-containing (SGC) cells of rat superior cervical ganglia. Histol Histopathol 1994 9 649-656. 

Pepsinogen appears to be excreted in characteristic amounts by each individual. The range in excretion of pepsinogen by normals was found to be from 0 to 136 units per hour.32 The acid phosphatase activities of male urines show a range of 5 to 310 units. Women excrete less, 5 to 70 units.33... 

Acid phosphatase (acid phosphomonoesterase, EC 3.1.3.2) also catalyzes the hydrolysis of phosphoric acid monoesters but with an acidic pH optimum. It has broad specificity and catalyzes transphosphorylations. Acid phosphatases are a quite heterogeneous group with monomeric, dimeric, larger glycoprotein, and membrane-bound forms. Acid phosphatase activity is present in the heart, liver, bone, prostate, and seminal fluid. Prostate carcinomas produce large quantities of acid phosphatase, and the enzyme is, therefore, used as a biomarker [141]. 

Chronic in vivo hemolysis produces serum lactic dehydrogenase elevations in patients with mitral or atrial valve cardiac prosthesis (J2). In a series of 11 such patients these increases ranged from 1.1 to 1.6 times the upper limit of normal (S29). Blood pH is altered in hemolyzcd specimens because carbonic anhydrase is liberated from the erythrocytes and presumably alters the distribution of H2CO3 and NaHCOs (B2). Hemolysis will effect acid phosphatase activity if the substrate is hydrolyzed by erythrocyte acid phosphatase. Thus, hemolysis would be of concern if phenyl phosphate was the substrate, but would have a negligible effect if )8-glycerophosphate, which is not hydrolyzed by red cell acid phosphatase, was used (Bl). 

The pH of serum, after it is separated from the clot, tends to go up as carbon dioxide is evolved and will eventually reach pH 8.5. This is an important consideration in the determination of acid phosphatase, which is rapidly destroyed at alkaline pH (W16a). Eighty-nine percent of serum acid phosphatase activity remains after 4 hours at pH 7.8 or 1 hour at pH 7.98 (B2). At pH 7.98 only 58% remains after 4 hours (B2). If serum is maintained over the clot, no rise in pH or inactivation of acid phosphatase occurs for as long as 5 hours at room temperature or 24 hours in the refrigerator (B17b). 

Testicular effects were also investigated after oral administration of 2000 mg/kg bw di(2-ethylhexyl) phthalate for seven consecutive days to 13-week-old male Wistar rats (Saxena et al., 1985). Degeneration was observed in about 40% of the seminiferous tubules. Loss of succinic dehydrogenase, NADH-diaphorase and acid phosphatase activity and increases in adenosine triphosphatase, glucose-6-phosphate dehydrogenase and alkaline phosphatase activity were observed in treated rats. 

Kidney Bean Purple Acid Phosphatase Active Site... 

Acid phosphomonoesterase (EC 3.1.3.2). Milk contains an acid phosphatase which has a pH optimum at 4.0 and is very heat stable (LTLT pasteurization causes only 10-20% inactivation and 30 min at 88°C is required for full inactivation). Denaturation of acid phosphatase under UHT conditions follows first-order kinetics. When heated in milk at pH 6.7, the enzyme retains significant activity following HTST pasteurization but does not survive in-bottle sterilization or UHT treatment. The enzyme is not activated by Mg2+ (as is alkaline phosphatase), but it is slightly activated by Mn2+ and is very effectively inhibited by fluoride. The level of acid phosphatase activity in milk is only about 2% that of alkaline phosphatase activity reaches a sharp maximum 5-6 days post-partum, then decreases and remains at a low level to the end of lactation. 

The acid phosphatase activity in milk increases by a factor of 4-10 during mastitic infection three isoenzymes are then present, only one of which is indigenous milk acid phosphatase, the other two being of leucocyte origin these latter isoenzymes are more thermolabile and are inactivated by HTST pasteurization. 

In 1924, Martland et al. (1) reported on phosphatase activity in red blood cells. Roche later differentiated between the phosphatase of the red cells with pH optimum 6.0-6.2 and the phosphatase from white cells with optimum 8.8-9.0. Roche also showed that a-glycerophosphate was split more rapidly than -glycerophosphate by red cell extracts while the reverse was true of acid phosphatase activity in plasma (2). While studying the source of acid phosphatase activity in male urine, Kutscher and Wolberg discovered the very high activity of acid phosphatase in human prostate (3). This tissue was shown by Woodard to have one-thousand times the activity of extracts from bone, liver, and kidney (3a). Igarashi and Hollander crystallized the acid phosphatase of rat liver and showed that under certain conditions allosteric control of the activity could be demonstrated (4). 

Beckman et al. (28) have studied the electrophoretic separation of the acid phosphatase activity in tissue extracts on starch gel at pH 8. They described four electrophoretic bands A, B, C, and D. Table IV (28) shows the distribution of activity in different organ extracts. The ABD pattern predominated in kidney BD in liver, intestine, heart, and skeletal muscle B in skin and D in pancreas. The C component was present in a large number of placentae but not in other adult organs. All four electrophoretic components were inhibited by d-(- -)-tartrate A contained sialic acid, D had a lower pH optimum and was more heat resistant than A, B, and C. Components C and D showed parallel electrophoretic behavior. In human skin fibroblasts grown in tissue culture, the acid phosphatase was generally high and the most common pattern was BD. Almost every culture showed some activity. The BD... 

Study of intermittent effluxes of acid phosphatase activity in the urine of mature human males 29) led to the discovery of the enzyme in semen and prostate by Kutscher and Wolberg (S). The enzyme is very active in human prostatic tissue and the caudal lobe of the rhesus monkey. Dog prostate contains much less enzyme than human tissue. Cat, guinea pig, rabbit, and rat prostates contain little (SO). Synthesis... 

Fig. 1. Prostatic acid phosphatase activity as a function of pH ( ) phenyl phosphate (O) p-nitrophenyl phosphate and (A) /8-glycerophosphate. Buffers Ac, acetate Cit, citrate and tris. From Nigam et al. (88).

Fig. 8. Sephadex G-200 gel filtration diagram of the acid phosphatase activity. There are two peaks, corresponding to the two immunologically different molecular forms of the enzyme. From S. Mattila, Invest. Urol. 6, 337 (1969). Copyright (1969), The Williams Wilkins Co., Baltimore, Maryland.

Fig. 13. The distribution of red cell acid phosphatase activities in a randomly selected English population (dotted line) and in the separate phenotypes. From Hopkinson and Harris (85).

In formalin-fixed rat liver, acid phosphatase activity is localized in peribiliary granules in the hepatic cells and in the Kupffer cells. The... 

Fia. 14. Polyacrylamide gel electrophoresis at various purification steps. Gels 1 to 4 were stained for acid phosphatase activity gel 5 was stained for protein. A current of 4 mA/gel was applied to gels 1-3 for 2 hr and to gels 4 and 5 for 6 hr. Gel 1, homogenate 2, DEAE-cellulose peak II 3, DEAE-cellulose peak I 4 and 5, crystalline enzyme. From Igarashi and Hollander (4). 

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