Acid Phosphatase In Tissue Research Articles

Relationship between acid phosphatase activity and P concentration in organs of Cyclopia and Aspalathus species, and a non-legume of the Cape Floristic Region

The role of tissue acid phosphatase (APase) activity of legumes and non-legumes in their P nutrition and adaptation to low-P soils is not well understood. To better understand this, a relationship between APase activity and P concentration in leaves, stems, roots and nodules of legumes, Cyclopia and Aspalathus and a non-legume, Leucadendron strictum, all native to the P-poor soils of the Cape fynbos biome, was assessed. Plants were collected and each separated into leaves, stems and roots. Phosphatase enzyme activity was assayed in soil using the p-nitrophenol method, while soil P and shoot P were measured using ICP-MS. To measure tissue APase activity, an acetate buffer was added into ground plant material and contents filtered. An acetate buffer and a p-nitrophenyl solution were added to the supernatant and contents incubated. After incubation, NaOH (0.5 M) was added and absorbance read at 405 nm. At Koksrivier, Cyclopia genistoides exhibited the highest leaf enzyme activity whilst Aspalathus aspalathoides showed the highest enzyme activity in the stems. At both Kleinberg and Kanetberg, Cyclopia subternata and Cyclopia longifolia showed the highest APase activity in leaves, followed by stems and lowest in roots. P concentration closely mirrored enzyme activity in organs of all test species from each site. APase activity positively correlated with P concentration in organs of all the test Cyclopia and Leucadendron species, indicating that intracellular APase activity is directly linked to P mobilization and translocation in these species. Percentage of N derived from fixation was positively correlated with tissue APase activity in C. genistoides (r = 0.911*), A. aspalathoides (r = 0.868*) and Aspalathus caledonensis (r = 0.957*), suggesting that APase activity could be directly or indirectly linked to symbiotic functioning in these fynbos legumes, possibly via increased P supply to sites of N₂ fixation.

Changes in P accumulation, tissue P fractions and acid phosphatase activity of Pilea sinofasciata in poultry manure-impacted soil

Pilea sinofasciata is a promising phytoextraction material to remove excess phosphorus (P) from manure-impacted soil. However, little information is available on its physiological response to animal manure treatments. Here, P accumulation, tissue P fractions and acid phosphatase activity were investigated in a mining ecotype (ME) and a non-mining ecotype (NME) of P. sinofasciata at different poultry manure (PM) treatments (0, 25, 50, 75, 100 and 125 g kg−1). Biomass and P accumulation of the ME increased up to 50 g kg−1, after which they significantly decreased; while P accumulation of the NME increased up to 100 g kg−1. But, shoot and root P accumulation of the ME were significantly higher than those of the NME at all PM treatments, showing 1.13–2.92 and 1.11–2.89 times higher values, respectively. Inorganic P and nucleic P dominated in tissues of both ecotypes. Besides, the ME maintained higher concentrations of inorganic P and ester P in leaves and ester P, nucleic P and residual P in roots than the NME. Acid phosphatase activity in leaves and roots increased by increasing PM treatments, except in root at 125 g kg−1. Acid phosphatase activity in leaves of the ME was positively correlated with concentrations of inorganic P, ester P and nucleic P, while that of the NME only correlated with inorganic P concentration. Probably, the optimized P fractions allocation and higher tissue acid phosphatase allow the ME to grow well and efficiently accumulate P in PM-impacted soil.

The effects of diversified phosphorus nutrition on the growth of oat (Avena sativa L.) and acid phosphatase activity

We studied the effect of differential phosphorus (P) supply on the development of oat seedlings (<em>Avena sativa</em> L. ‘Arab’) as well as localization and activity of acid phosphatases in tissues and root exudates. Plants were grown for 1–3 weeks on nutrient media with inorganic phosphate (+P, control), reduced Pi (0.1 P), phytic acid (PA) as organic P source, and without P addition (−P), in standard conditions or in a split-root culture system. Phosphate starvation reduced shoot growth but increased root elongation and root/shoot ratio, whereas 0.1 P and PA oat plants had similar growth parameters to +P plants. The growth on −P medium significantly decreased Pi content in all tissues, but only a slight Pi decrease was observed in plants grown on 0.1 P and PA media or various split-root system conditions. Pi starvation led to an increase in acid phosphatase (APase) activity in root exudates when compared to +P, 0.1 P, and PA plant samples. APase activity was especially intensive in root cross sections in rhizodermis and around/in vascular tissues of −P plants. For plants grown on 0.1 P medium and on phytic acid, APase activity did not change when compared to the control. Three major isoforms of APases were detected in plant tissues (similar in all studied conditions, with a higher activity of one isoform under Pi deficit). Generally, lowered Pi content (0.1 P) was not stressful to oat plants for up to 3 weeks of culture. Oat plants grew equally well on nutrient media with Pi and on media with phytate, although phytate was considered not available for other plants. The oat plants activated mainly extracellular APases, but also intracellular enzymes, rather via nonlocal signals, to acquire Pi from external/internal sources under Pi deficiency.

Effect of P and biostimulant application on growth and tissue acid phosphatase activity of desi and kabuli chickpea at Klipplaatdrift, South Africa

Effect of P and biostimulant application on growth and tissue acid phosphatase activity of desi and kabuli chickpea at Klipplaatdrift, South Africa

Histochemical Distribution of Acid phosphatase in the tissues of Indian Major carp, Labeorohita (ham)

Acid phosphatases (AcPs) are known to provide phosphate to tissues that have high energy requirements, especially during development, growth and maturation. AcPs enzyme shows variations in quantity in reproductive phases in gonads, kidney and liver. AcPs is highest in both the sexes in postspawning phase and lowest in preparatory phase. In male, acid phosphatase activity is maximum in all three tissues i.e gonads, kidney and liver in postspawning phase and lowest in the preparatory phase as in female. AcPs staining was either granular or in diffuse form in brown deposits. This study is aimed on the estimation of activity of acid phosphatase in kidney, liver and gonads tissues of Labeorohita

Caracterização isoenzimática de genótipos de arroz

Objetivou-se, neste trabalho, caracterizar isoenzimaticamente genótipos de arroz (Oryza sativa L.). A produtividade do arroz irrigado no Rio Grande do Sul é elevada, em virtude da alta tecnologia e sistema de irrigação usados, associados ao potencial alcançado pelas cultivares desenvolvidas através de melhoramento genético. Apenas seis ancestrais contribuem com 86% dos genes das cultivares mais plantadas. Como conseqüência desta estreita base genética, as cultivares apresentam um alto grau de parentesco e de similaridade de suas características morfológicas e agronômicas, o que dificulta a identificação varietal. A concorrência com genótipos, como arroz-vermelho e arroz-preto, de difícil controle por serem da mesma espécie que os cultivados, é considerada como um dos maiores problemas da cultura. Análises de isoenzimas podem ser usadas para o estudo da variabilidade e para estimar as relações genéticas existentes entre estes genótipos. Eletroforese em gel de poliacrilamida foi empregada, portanto, para caracterizar, através de isoenzimas de esterase, 6fosfogluconato desidrogenase, fosfoglucoisomerase e isocitrato desidrogenase em sementes e folhas de plântulas, e de fosfatase ácida e aspartato transaminase em folhas de plântulas, as cultivares BR-IRGA 409, BR-IRGA 410, BRS 6 ('Chuí'), BRS 7 ('Taim'), BRS Agrisul, INIA Taquari, El Paso L 144 e IRGA 417, e ecótipos de arroz-vermelho e arroz-preto. A análise de agrupamento, efetuada por meio do coeficiente de Jaccard e pelo método da média aritmética não ponderada (UPGMA), possibilitou a diferenciação de todos os genótipos, à exceção de BRS 6 ('Chuí') e BRS 7 ('Taim'). Três grupos foram identificados, incluindo-se, em um deles, os ecótipos de arroz-vermelho e arroz-preto, que apresentaram 95% de similaridade.

Genetic polymorphism of rabbit (Oryctolagus cuniculus) tissue acid phosphatases (ACP2 and ACP3)

Rabbit ( Oryctolagus cuniculus) red cell and tissue acid phosphatases were studied by means of horizontal starch gel electrophoresis and isoelectric focusing followed by enzyme blotting. Red cell acid phosphatase 1 (ACP1) is monomorphic while tissue acid phosphatase 2 (ACP2) is polymorphic in a wild rabbit population, with two alleles: ACP2*1 (0.96) and ACP2*2 (0.04). A third locus homologous of human acid phosphatase 3 (ACP3) is characterized by the presence of three alleles (ACP3*1, ACP3*2 and ACP3*3). ACP3*1 is the most common allele and was detected in all populations, ACP3*2 was found in domestic breeds and in a wild population from Southern France, whereas ACP3*3 is typical of Portuguese wild rabbits. The geographical distribution of ACP3*2 and ACP3*3 is in agreement with the subspecific level of differentiation of the rabbit species in O. cuniculus cuniculus and O. c. algirus. The comparative study of the acid phosphatase activity in red cells of several mammalian species, including humans, suggests that ACP3 activity in erythrocytes exists only in rabbit.

Short term in vivo method for prediction of the fibrogenie effect of different mineral dusts

The effect of intratracheal introduction of different metal and mineral dusts and the change in activity of pulmonary acidic phosphatase have been studied as a function of time (72 h, 2 weeks, 1, 12, 20 months). The activity and localization of acid phosphatase were compared with the degree of pulmonary damage caused by dusts. The degree of fibrosis was determined on the basis of the composition of cells and fibres, according to Belt and King's classification. Due to the membrane-damaging effect of DQ 12 silica and mixed dusts (enargite and porphyry rock dusts) an increase in acid phosphatase activity of macrophages could be observed at the end of the first month. At the same time non-fibrogenic or only mild fibrogenic dusts (bentonite, corundum, scarnic rock dust) caused a decrease or disappearance of tissue acid phosphatase activity. It has been stated that there is a very close correlation between the change in pulmonary acidic phosphatase activity and the progression of pulmonary fibrosis due to exposure to mineral dusts. The above investigations have been most useful in predicting the subsequent effect of rock patterns, emphasizing at the same time the importance of in vivo long term experiments.

Acid phosphatase in Gaucher's disease.

Abstract Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.

Acid phosphatase in Gaucher's disease.

Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.

A new treatment for ischemic bowel disease: Steroid delivery via retrograde venous route

The present therapeutic approach to occlusive mesenteric disease is unable to alter its high mortality and morbidity. We attempted to stabilize the intestinal lysosomal population with steroid prior to revascularization and thus reduce the lysosomal effluent. Steroid delivery during the occlusive period was accomplished via retrograde venous flow in the portal system. During revascularization steroid was further infused via the superior mesenteric artery. Our experimental model compared systemic venous delivery with retrograde portal venous delivery of steroid. Analysis of tissue acid phosphatase levels suggested steroid delivery via retrograde portal venous flow is the most efficient method of lysosomal stabilization.

Inhibition of human prostatic tumour acid phosphatase by N,N-p-di-2-chloroethylaminophenol, N,N-p-di-2-chloroethylaminophenyl phosphate and other difunctional nitrogen mustards

Potent inhibition of human prostatic carcinoma tissue acid phosphatase by N,N-p-di-2-chloroethylaminophenol (AMOH) and N,N-p-di-2-chloroethylaminophenyl phosphate (AMPh) is described. Certain other difunctional nitrogen mustards were also inhibitory but N,N-p-di-2-hydroxyethylaminophenol, the non-alkylating fully hydrolysed product from AMOH, was not. Inactivation of the enzyme by AMPh was progressive with time, showed apparent first order reaction kinetics and was not reversed by extensive dialysis. The results suggest that the inability of the enzyme to catalyse the hydrolysis of AMPh was due to inhibition in the presence of AMPh, possibly involving an alkylating mechanism. The implications for possible chemotherapy with AMPh are discussed.

Isatin Enzyme Interactions

Influence of Isatin on rat tissue acid phosphatase has been studied. It has an organ-specific effect, the liver enzyme is activated, the brain enzyme is inhibited while those of kidney and intestine are not affected. Isatin activation of the liver enzyme is of mixed type and pH dependent. Rat liver enzyme appears to require intact amino and sulfhydryl groups for activity. Isatin seems to combine with the enzyme through the sulfhydryl group of the latter.

The distribution of acid phosphatase in the Tasmanian devil, Sarcophilus harrisii (marsupialia; dasyuridae)

1.1. Serum and tissue acid phosphatase concentrations were determined in male and female Sarcophilus harrisii.2.2. Serum levels in both sexes greatly exceeded human values.3.3. Tissue levels of the enzyme were high particularly in reticulo-endothelial and reproductive organs.4.4. Two forms of a.p.∗ were identified by their response to formalin and the quantities of these are given for serum and tissue.5.5. Formalin resistant a.p. (so called prostatic) was found in both sexes. To avoid confusion it is suggested that the term prostatic a.p. be replaced by formalin-resistant a.p.

Histochemical enzyme studies of prostatic carcinoma influenced by therapy

Perineal puncture procured material from 10 patients with clinically and microscopically proven prostatic cancer, both before and after intensive female-hormonal therapy and after castration; the tissues were studied histochemically and microscopically. Apart from tissue acid-phosphatase, the following were investigated: succino-dehydrogenase (SDH), isocitrate-dehydrogenase (LCDH), β-hydroxybutyrate-dehydrogenase (β-BDH), glucose-6-phosphate-dehydrogenase (G-6-PDH), glutamate-dehydrogenase (GDH), lactate-dehydrogenase (LDH). Following hormonal therapy and castration there was, in both the solid cancer and in adenocarcinoma, a readily demonstrable fall of enzymatic activity compared to that at initial puncture. Striking was the transition to dedifferentiation of the adenocarcinoma following hormonal therapy and castration despite improvement in clinical palpation. In the presence of negative stromal reaction, the tumor cells of the dedifferentiated cancer there was obvious activity of the GDH, LDH, β-BDH and acid phosphatase. There was slight to no activity of citrate and pentose-phosphate cycle. Two patients with histologically dedifferentiated carcinoma and adenocarcinoma, respectively, after second puncture, showed no evidence of cancerous tissues while at the same time evincing limitation of enzymatic activity (LDH) to the smooth muscle.

Lysosomes and acid phosphatases during growth and differentiation in mice: a light and electron microscope study.

The activity of acid phosphatase in tissues of young and adult animals was investigated at the optical and ultrastructural levels using naphthol AS-BI phosphate as a substrate. Incubation of tissues in the presence of sodium molybdate and sodium fluoride was used to investigate the localization of a second acid phosphatase which is not inhibited by these compounds.

Acid-phosphatase activity in human neoplasms

CancerVolume 10, Issue 3 p. 563-576 ArticleFree Access Acid-phosphatase activity in human neoplasms Leopold Reiner M.D., Leopold Reiner M.D. Departments of Surgery and Pathology, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts Departments of Pathology, Bronx Hospital and Albert Einstein College of Medicine, New York, New York Departments of Surgery, Sinai Hospital of Baltimore and the Johns Hopkins University School of Medicine, Baltimore, MarylandSearch for more papers by this authorAlexander M. Rutenburg M.D., Alexander M. Rutenburg M.D. Departments of Surgery and Pathology, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts Departments of Pathology, Bronx Hospital and Albert Einstein College of Medicine, New York, New York Departments of Surgery, Sinai Hospital of Baltimore and the Johns Hopkins University School of Medicine, Baltimore, MarylandSearch for more papers by this authorArnold M. Seligman M.D., Arnold M. Seligman M.D. Departments of Surgery and Pathology, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts Departments of Pathology, Bronx Hospital and Albert Einstein College of Medicine, New York, New York Departments of Surgery, Sinai Hospital of Baltimore and the Johns Hopkins University School of Medicine, Baltimore, MarylandSearch for more papers by this author Leopold Reiner M.D., Leopold Reiner M.D. Departments of Surgery and Pathology, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts Departments of Pathology, Bronx Hospital and Albert Einstein College of Medicine, New York, New York Departments of Surgery, Sinai Hospital of Baltimore and the Johns Hopkins University School of Medicine, Baltimore, MarylandSearch for more papers by this authorAlexander M. Rutenburg M.D., Alexander M. Rutenburg M.D. Departments of Surgery and Pathology, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts Departments of Pathology, Bronx Hospital and Albert Einstein College of Medicine, New York, New York Departments of Surgery, Sinai Hospital of Baltimore and the Johns Hopkins University School of Medicine, Baltimore, MarylandSearch for more papers by this authorArnold M. Seligman M.D., Arnold M. Seligman M.D. Departments of Surgery and Pathology, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts Departments of Pathology, Bronx Hospital and Albert Einstein College of Medicine, New York, New York Departments of Surgery, Sinai Hospital of Baltimore and the Johns Hopkins University School of Medicine, Baltimore, MarylandSearch for more papers by this author First published: May/June 1957 https://doi.org/10.1002/1097-0142(195705/06)10:3<563::AID-CNCR2820100321>3.0.CO;2-ICitations: 43AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL References 1 Berthet, J., and de Duve, C.: Tissue fractionation studies; existence of mitochondria-linked, enzymatically inactive form of acid phosphatase in rat-liver tissue. Biochem. J. 50: 174– 181, 1951. 2 Gomori, G.: Distribution of acid phosphatase in tissues under normal and under pathologic conditions. Arch. Path. 32: 189– 199, 1941. 3 Grogg, E., and Pearse, A. G. E.: Critical study of histochemical techniques for acid phosphatase, with description of azo-dye method. J. Path. & Bact. 64: 627– 636, 1952. 4 Lemon, H. M.; Davison, M. M., and Asimov, I.: Acid-phosphatase activity of normal and neoplastic human tissues. Cancer 7: 92– 99, 1954. 5 Newman, W.; Kabat, E. A., and Wolf, A.: Histochemical studies on tissue enzymes; difficulty in enzyme localization in acid range due to selective affinity of certain tissues for lead: its dependence on pH. Am. J. Path. 26: 489– 503, 1950. 6 Palade, G. E.: Intracellular localization of acid phosphatase; comparative study of biochemical and histochemical methods. J. Exper. Med. 94: 535– 548, 1951. 7 Reiner, L.; Wittels. B.; Barrnett, R. J., and Rutenburg, A. M.: Histochemical profile of human myocardium in coronary artery disease. [Abstr.] J. Histochem. & Cytochem. 3: 409– 410, 1955. 8 Rutenburg, A. M., and Seligman, A. M.: Histochemical demonstration of acid phosphatase by postincubation coupling technique. J. Histochem. & Cytochem. 3: 455– 470, 1955. 9 Woodard, H. Q., and Dean, A. L.: Significance of phosphatase findings in carcinoma of prostate. J. Urol. 57: 158– 171, 1947. Citing Literature Volume10, Issue3May/June 1957Pages 563-576 ReferencesRelatedInformation

Acid phosphatase activity in the intestinal wall in experimental amebic colitis.

Acid phosphatase activity has been demonstrated in Endamoeba histolytica of human origin grown in artificial culture media or obtained by rectal aspiration from an experimentally infected animal(1). The present report describes the results obtained when tissue sections of amebic lesions were submitted to the acid phosphatase test.Materials and methods. Amebic colitis was experimentally produced in guinea pigs by intra-ileal inoculation with large numbers (over 200,000) of amebic trophozoites (Tulane strain XXII) grown in Balamuth's medium(2). Four to 7 days after inoculation the animals were sacrificed and portions of cecum with extensive amebic lesions were selected for study. Gomori's histochemical technic for the demonstration of acid phosphatase in tissue(3) was used throughout the experiment. Duplicate sections submitted to identical procedure except for the absence of the glycerophosphate substrate from the incubating solution, served as controls. All sections were incubated overnight.Results. Very ...

Post-Mortem Findings in Carcinoma of the Prostate Following Castration and Diethylstilbestrol Therapy: A Case Report with Autopsy and Post-Mortem Tissue Acid Phosphatase Studies

No AccessJournal of Urology1 Jul 1943Post-Mortem Findings in Carcinoma of the Prostate Following Castration and Diethylstilbestrol Therapy: A Case Report with Autopsy and Post-Mortem Tissue Acid Phosphatase Studies George G. Gilbert and George Margolis George G. GilbertGeorge G. Gilbert More articles by this author and George MargolisGeorge Margolis More articles by this author View All Author Informationhttps://doi.org/10.1016/S0022-5347(17)70421-1AboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareFacebookLinked InTwitterEmail © 1943 by The American Urological Association Education and Research, Inc.FiguresReferencesRelatedDetailsCited byMuhsen J (2018) Possible Significance of the Prostatic Secretion Acid Phosphatase as a Diagnostic and a Prognostic Index in Carcinoma of the ProstateJournal of Urology, VOL. 72, NO. 5, (928-933), Online publication date: 1-Nov-1954. Volume 50Issue 1July 1943Page: 82-94 Advertisement Copyright & Permissions© 1943 by The American Urological Association Education and Research, Inc.MetricsAuthor Information George G. Gilbert More articles by this author George Margolis More articles by this author Expand All Advertisement PDF downloadLoading ...

Theory and Application of the Serum “acid” Phosphatase Determination in Metastasizing Prostatic Carcinoma; Early Effects Of Castration

No AccessJournal of Urology1 Oct 1942Theory and Application of the Serum “acid” Phosphatase Determination in Metastasizing Prostatic Carcinoma; Early Effects Of Castration Thomas J. Sullivan, Ethel Benedict Gutman, and Alexander B. Gutman Thomas J. SullivanThomas J. Sullivan More articles by this author , Ethel Benedict GutmanEthel Benedict Gutman More articles by this author , and Alexander B. GutmanAlexander B. Gutman More articles by this author View All Author Informationhttps://doi.org/10.1016/S0022-5347(17)70732-XAboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareFacebookLinked InTwitterEmail © 1942 by The American Urological Association Education and Research, Inc.FiguresReferencesRelatedDetailsCited ByBrawer M, Chetner M, Beatie J, Buchner D, Vessella R and Lange P (2018) Screening for Prostatic Carcinoma with Prostate Specific AntigenJournal of Urology, VOL. 147, NO. 3 Part 2, (841-845), Online publication date: 1-Mar-1992.Heller J (2018) Prostatic Acid Phosphatase: Its Current Clinical StatusJournal of Urology, VOL. 137, NO. 6, (1091-1103), Online publication date: 1-Jun-1987.Pontes J (2018) Biological Markers in Prostate CancerJournal of Urology, VOL. 130, NO. 6, (1037-1047), Online publication date: 1-Dec-1983.Romas N, Veenema R, Hsu K, Tomashefsky P, Lattimer J and Tannenbaum M (2018) Bone Marrow Acid Phosphatase in Prostate Cancer: An Assessment by Immunoassay and Biochemical MethodsJournal of Urology, VOL. 123, NO. 3, (392-395), Online publication date: 1-Mar-1980.Chu T (2018) Editorial CommentJournal of Urology, VOL. 123, NO. 3, (395-395), Online publication date: 1-Mar-1980.Veenema R, Gursel E, Romas N, Wechsler M and Lattimer J (2018) Bone Marrow Acid Phosphatase: Prognostic Value in Patients Undergoing Radical ProstatectomyJournal of Urology, VOL. 117, NO. 1, (81-82), Online publication date: 1-Jan-1977.Ishibe T, Usui T and Nihira H (2018) Prognostic Usefulness of Serum Acid Phosphatase Levels in carcinoma of the ProstateJournal of Urology, VOL. 112, NO. 2, (237-240), Online publication date: 1-Aug-1974.Lepow H, Schoenfeld M, Messeloff C and Chu F (2018) Non-prostatic Causes of Acid Hypekphosphatasia: Report of a Case Due to Multiple MyelomaJournal of Urology, VOL. 87, NO. 6, (991-993), Online publication date: 1-Jun-1962.Graves R, Desautels R and Warren S (2018) Hormone-Independent Cancer of the ProstateJournal of Urology, VOL. 79, NO. 2, (324-332), Online publication date: 1-Feb-1958.Ganem E (2018) The Prognostic Significance of an Elevated Serum Acid Phosphatase Level in Advanced Prostatic CarcinomaJournal of Urology, VOL. 76, NO. 2, (179-181), Online publication date: 1-Aug-1956.Ozar M, Isaac C and Valk W (2018) Methods for the Elimination of Errors in Serum Acid Phosphatase DeterminationsJournal of Urology, VOL. 74, NO. 1, (150-157), Online publication date: 1-Jul-1955.Stewart C, Sweetser T and Delory G (2018) A Case of Benign Prostatic Hypertrophy with Recent Infarcts and Associated High Serum Acid PhosphataseJournal of Urology, VOL. 63, NO. 1, (128-131), Online publication date: 1-Jan-1950.Fischmann J, Chamberlin H, Cubiles R and Schmidt G (2018) Quantitative Determinations of Acid Phosphatase in the Prostate Under Various Normal and Pathological Conditions: Preliminary ReportJournal of Urology, VOL. 59, NO. 6, (1194-1196), Online publication date: 1-Jun-1948.Woodard H and Dean A (2018) The Significance of Phosphatase Findings in Carcinoma of the ProstateJournal of Urology, VOL. 57, NO. 1, (158-171), Online publication date: 1-Jan-1947.Alyea E (2018) Early or Late Orchiectomy for Carcinoma of the ProstateJournal of Urology, VOL. 53, NO. 1, (143-153), Online publication date: 1-Jan-1945.Palomo A (2018) Carcinoma of the Prostate GlandJournal of Urology, VOL. 53, NO. 1, (166-187), Online publication date: 1-Jan-1945.Gilbert G and Margolis G (2018) Post-Mortem Findings in Carcinoma of the Prostate Following Castration and Diethylstilbestrol Therapy: A Case Report with Autopsy and Post-Mortem Tissue Acid Phosphatase StudiesJournal of Urology, VOL. 50, NO. 1, (82-94), Online publication date: 1-Jul-1943. Volume 48Issue 4October 1942Page: 426-458 Advertisement Copyright & Permissions© 1942 by The American Urological Association Education and Research, Inc.MetricsAuthor Information Thomas J. Sullivan More articles by this author Ethel Benedict Gutman More articles by this author Alexander B. Gutman More articles by this author Expand All Advertisement Loading ...