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Serum phosphatase

B15. Bodansky, A., Phosphatase studies Determination of serum phosphatase factors influencing the accuracy of the determination. J. Biol. Chem. 101, 93-104 (1933). [Pg.34]

In practice it is often more convenient to measure the release of a phenol from an aryl phosphomonoester. Standard serum phosphatase methods employ phenyl phosphate (188), p-nitrophenyl phosphate (189), phenolphthalein monophosphate (140), or thymolphthalein monophosphate (141) where the phenol released can be determined spectrophoto-metrically [only the Bodansky method (13) uses a Pi determination]. A number of fluorogenic substrates have been used for phosphatase studies, e.g., jS-naphthyl phosphate (30, 148), 4-methylumbelliferyl phosphate (143), and 3-O-methylfluorescein phosphate (144) The main advantage here is the much greater sensitivity of fluorescence as compared with spectrophotometric assays as little as 1 pmole of 4-methyl-umbelliferone can be detected in continuous assay. [Pg.433]

H21. Huggins, C., and Hodges, C. V., Studies on prostate cancer. 1. The effect of castration, of estrogen and of androgen injection on serum phosphatases in metastatic carcinoma of the prostate. Cancer Res. 1, 293-297 (1941). [Pg.148]

In 1956, Fishman et al. (F2) summed up their experience with a series of 91 cases of proven cancer of the prostate and a total of 1198 patients with other diseases. Of these 91 cases, 32, or 35%, had elevated total serum acid phosphatase activities. This incidence was much lower than that, 85%, reported by Sullivan et al. (S30) in 1942 or the value of 89% reported by Herbert (H5) in 1946 for patients with carcinoma of the prostate and skeletal metastases. These investigators had used the method of Gutman and Gutman (GIO, G14), which was essentially the same method as that employed by Fishman and Lerner (FI) and gave the same ranges of normal values (Table 6). The possibility existed that treated cases had normal total serum phosphatase activities and thus weighted the overall incidence toward a low value. However, the data of Fishman et al. (F2) show that the incidence of total serum acid phosphatase activities in treated cases was 20/52, or 38%, even higher than the incidence 12/39, or 31%, in the untreated cases. [Pg.109]

After infusion, iludarahine phosphate i.s rapidly dc )hiS phorylated by serum phosphatases and converted into 2-fIU oroadenosine arabinoside (2-FLAA). The levels of 2-RA4 decline biexponentially, with half-lives of 0.6 and 9.3 Iwiin 2-FLAA enters cells by a carrier-mediated process aik undergoes intracellular phosphorylation by dMxycylidinc kinase to the active form. 2-F-ara-ATP. " ... [Pg.412]

Previous work on human alkaline phosphatases has utilized chromatography (ElO) and starch-gel electrophoresis. Thus in 1956 Boman and Westlund (B34) reported the purification and separation of serum phosphatases by Dowex-2 column chromatography. Moss (M34) used gel filtration on Sephadex G-200 and DEAE-celluIose chromatography for separating 5 -nucleotidase and nonspecific alkaline phosphatase activities in human sera. In most of the studies of alkaline phosphatases in human tissues of liver (M33), intestine (M34, M35), bone (M36), kidney (B46), and urine (B44, B46, B47), crude extracts of these tissues were used and... [Pg.293]

It must be stressed that hyperphosphatasemia in uncomplicated liver or bone disease, although of academic interest, has never posed a mystery of interpretation to the clinician nor has it confused the grounds for his decision making. The problem has arisen principally in dealing with laboratory findings in coexisting liver and bone disease, especially where a sudden elevation has occurred in the serum phosphatase level, as in hormonal therapy of cancer of the breast or of the prostate. [Pg.342]

A18. Arfors, K. E., Beckman, L., and Limdin, L. G., Further studies on the association between human serum phosphatases and blood groups. Acta Genet. (Statist. Med.) 13, 366-368 (1963). [Pg.348]

B26. Bodansky, A., Non-osseous origins of serum phosphatase. Proc. Soc. ExpU. Biol. Med. 42, 800-804 (1939). [Pg.350]

D4. Dalgaard, J. B., Serum phosphatase after hepatectomy in dogs. Acta Physiol. Scand. 16, 308-317 (1949). [Pg.352]

D21. Doose, H., Studies uber die alkalische serum phosphatase der Ratte. D. Mittei-lung Das Verhalten der alkalischen serumphosphatase der rachitischen Ratte unter Vitamin D. Z. Exptl. Med. 184, 73-81 (1960). [Pg.353]

D22. Drill, V. A., and Riggs, D. S., Inhibition of alkaline serum phosphatase activity during liver disease. J. Biol. Chem. 162, 21-25 (1946). [Pg.353]

G16. Green, S., Giovanniello, T. J., and Fishman, W. H., Automated differential analysis of several serum phosphatase isoenzymes. Proc. Technicon Symp. Automation Anal. Chem., New York (in press). [Pg.356]

K14. Klees, E. and Frenzel, G., Zur problematik der erhohung der alkalischen serum phosphatase Aotivitat unter der Geburt und im Wechenbett. Klin. Wochschr. 88, 540-543 (1960). [Pg.358]

N7. Nath, R. L., and Ghosh, N. K., Studies on serum phosphatases Effect of dilution on acid and alkaline phosphatases of human serum. Enzymologia 26, 182-195 (1963). [Pg.362]

R4. Rendel, J., and Stonnont, C., Variants of ovine alkaline serum phosphatases and their association with the R-0 blood groups. Proc. Soc. Exptl. Biol. Med. 116, 853-856 (1964). [Pg.365]

B29. Bodansky, A., Notes on the determination of serum inorganic phosphate and serum phosphatase activity. ]. Biol. Chem. 120, 167-175 (1937). [Pg.220]

B30. Bodansky, A., and Jaffe, H. L., Phosphatase studies. HI. Serum phosphatase in diseases of the bone. Interpretation and significance. Arch. Intern. Med. 54, 88-110 (1934). [Pg.220]

DIO. Drill, V. A., and Ivy, A. O., Comparative value of bromsulphthalein, serum phosphatase, prothrombin time and intravenous galactose tolerance tests in detecting hepatic damage produced by carbon tetrachloride. J. Clin. Invest. 23, 209-216 (1944). [Pg.370]

G8. Gould, B. S., and Shwachman, H., Bone and tissue phosphatase in experimental scurvy and studies on the source of serum phosphatase. Am. J. Physiol. 136, 485-491 (1942). [Pg.194]

Bodansky A, Jaffe HL, Chandler JP. 1932. Serum phosphatase changes in calcium deficiency and in ammonium chloride osteoporosis. Proc Soc Exp Biol Med 29 871-873. [Pg.183]


See other pages where Serum phosphatase is mentioned: [Pg.1362]    [Pg.597]    [Pg.496]    [Pg.175]    [Pg.125]    [Pg.322]    [Pg.348]    [Pg.2427]    [Pg.219]    [Pg.220]    [Pg.221]    [Pg.231]    [Pg.234]    [Pg.238]    [Pg.241]    [Pg.243]   


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