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PubMed1985

Prognostic significance of alkaline and acid phosphatase and skeletal scintigraphy in carcinoma of the prostate.

The prognostic significance of skeletal scintigraphy has been reassessed in relation to other tests by extended follow-up of 220 patients. Skeletal metastases increased in prevalence with T stage and were associated with shorter survival irrespective of age. Early disease, a normal acid or alkaline phosphatase at presentation and well differentiated tumours were associated with longer survival. Alkaline phosphatase alone accounted for all of the differences in survival. Scintigraphic change preceded elevation of the prostatic acid phosphatase in 81% of the patients whose initial scintigraphy and prostatic acid phosphatase were normal but who developed evidence of distant metastases on follow-up. The mean interval between scintigraphic conversion and the development of overt symptoms was 5.8 months. Our findings discount the value of skeletal scintigraphy for determining prognosis but do indicate that it is more sensitive than the acid phosphatase in identifying patients before they become symptomatic. Scintigraphy is indicated as a routine staging procedure in all new patients with carcinoma of prostate. In patients with a normal alkaline phosphatase, a baseline and regular follow-up are needed to identify patients likely soon to develop symptoms. If the alkaline phosphatase is elevated at presentation, scintigraphy is necessary to distinguish benign from malignant causes and to determine the extent of skeletal involvement.

Acid Phosphatase↗
PubMed1972

Alkaline and acid phosphatase in murine leukemia.

Alterations for acid and alkaline phosphatase levels and their pattern of splenic and lymph node activity in normal and virus-induced lymphoblastic leukemia were studied. Enzyme levels were examined by using both cytochemical and biochemical procedures. The GC leukemia virus, a ribonucleic acid murine virus antigenically related to the Rauscher-Moloney viruses, was used to stimulate acid and alkaline phosphatase by producing lymphomaceous disease in Ha/ICR mice. With the Burstone and Gomori cytochemical procedures, both enzymes were found in higher than normal levels in lymphomaceous spleen and lymph nodes. Confirmation of the cytochemical studies was obtained by enzyme assay of cell-free homogenates in each case with the exception of spleen acid phosphatase. The discrepancy between the cytochemical tests which showed significant elevation of spleen acid phosphatase and the enzyme assays which failed to reveal such elevation could be due to a labile acid phosphatase isozyme which is lost on cellular disruption during homogenate preparation. A significant spleen alkaline phosphatase specific activity elevation above normal was found with a 50% incidence only when leukemic spleen wet weight increased nearly threefold its normal value. This result suggests that alkaline phosphatase elevation is a secondary event occuring after the onset of disease and is not a fundamental metabolic alteration concerned with the onset of murine lymphoblastic leukemia.

Acid Phosphatase↗
PubMed1964

EVIDENCE FOR AN EXOCELLULAR SITE FOR THE ACID PHOSPHATASE OF SACCHAROMYCES MELLIS.

Weimberg, Ralph (Northern Regional Research Laboratory, Peoria, Ill.), and William L. Orton. Evidence for an exocellular site for the acid phosphatase of Saccharomyces mellis. J. Bacteriol. 88:1743-1754. 1964.-Evidence is presented which demonstrates an exocellular location for acid phosphatase in Saccharomyces mellis. Derepressed intact cells exhibit acid phosphatase activity. The properties of the system are similar to those shown by the enzyme in cell-free extracts. There is no increase in total activity when cell-free extracts are prepared. Enzymatically active cell walls were prepared by leaching acetone-dried cells of this yeast in dilute acetate buffer (pH 6.5) plus beta-mercaptoethanol. The insoluble residue, consisting mainly of cell-wall material and containing the phosphatase, was treated with a variety of hydrolytic enzymes and other chemicals. Only papain and crude snail gut extracts dissociated the enzyme from the particulate fraction in nearly quantitative amounts. The mechanism of release by these two enzymes probably differs. Of all enzymes tested, only the snail gut extract digested the cell walls. By dividing the procedure for making protoplasts of S. mellis into two steps, acid phosphatase may be dissociated from resting cells and recovered as an active soluble enzyme. The first step is to pretreat the cells with a thiol reagent. The second step is to digest the cell wall by enzymes present in crude snail gut extracts. Arsenite must be included in the second step to protect the phosphatase from inactivation. The phosphatase is quantitatively released before the cell becomes osmotically fragile.

Acid Phosphatase↗
PubMed1988

The epidermal growth factor receptor from prostate cells is dephosphorylated by a prostate-specific phosphotyrosyl phosphatase.

Human prostatic acid phosphatase (PAcP) has been found to have phosphotyrosyl-protein phosphatase activity (H. C. Li, J. Chernoff, L. B. Chen, and A. Kirschonbaun, Eur. J. Biochem. 138:45-51, 1984; M.-F. Lin and G. M. Clinton, Biochem. J. 235:351-357, 1986) and has been suggested to negatively regulate phosphotyrosine levels, at least in part, by inhibition of tyrosine protein kinase activity (M.-F. Lin and G. M. Clinton, Adv. Protein Phosphatases 4:199-228, 1987; M.-F. Lin, C. L. Lee, and G. M. Clinton, Mol. Cell. Biol. 6:4753-4757, 1986). We investigated the molecular interaction of PAcP with a specific tyrosine kinase, the epidermal growth factor (EGF) receptor, from prostate carcinoma cells. Of several proteins phosphorylated in membrane vesicles from prostate carcinoma cells, PAcP selectively dephosphorylated the EGF receptor. The prostate EGF receptor was more efficiently dephosphorylated by PAcP than by another phosphotyrosyl phosphatase, potato acid phosphatase. Further characterization of the interaction of PAcP with the EGF receptor revealed that the optimal rate of dephosphorylation occurred at neutral rather than at acid pH. Thus, the enzyme that we formerly referred to as PAcP we now call prostatic phosphotyrosyl-protein phosphatase. Hydrolysis of phosphate from tyrosine residues in the immunoprecipitated EGF receptor catalyzed by purified prostatic phosphotyrosyl-protein phosphatase caused a 40 to 50% decrease in the receptor tyrosine kinase activity with angiotensin as the substrate. In contrast, autophosphorylation of the receptor was associated with an increase in tyrosine kinase activity.

Adenocarcinoma↗
PubMed1999

Identification of sds21 in fission yeast in an inhibitor-resistant high molecular mass protein phosphatase-1 complex.

While characterizing the type-1 protein phosphatases sds21 and dis2 in fission yeast (Schizosaccharomyces pombe) a novel high molecular mass protein was identified with serine/threonine phosphatase activity (referred to as PP-R) that was resistant to a panel of characteristic inhibitors of protein phosphatases. Purification of the native sds21 catalytic isoform of protein phosphatase-1 (PP-1) from an S. pombe knockout strain lacking dis2 (deltadis2) resulted predominantly in identification of PP-R. To test the hypothesis that the catalytic activity of PP-R comprised sds21, a parallel purification was performed of PP-1 activity from an S. pombe knockout strain lacking sds21 (deltasds21). Both deltasds21 and deltadis2 strains exhibited similar protein phosphatase activity profiles as determined by DEAE-sepharose, Mono-Q and Superdex gel filtration chromatography. However, the peak of protein phosphatase activity from deltasds21 S. pombe that co-migrated with PP-R from deltadis2 S. pombe exhibited the sensitivity to a panel of inhibitors that was characteristic of a type-1 protein phosphatase. These data suggest that the catalytic subunit of PP-R comprises sds21 and that the resistance to inhibitors may originate from structural differences between dis2 and sds21 isoforms. A key structural feature present in sds21, but lacking in dis2, is a classical phosphorylation consensus sequence surrounding serine-145 of sds21. The previous hypothesis was that PP-1 activity among several lower eukaryotes may be regulated directly by cAMP-dependent protein kinase (PKA) phosphorylation. However, this study demonstrated that recombinant sds21 is not a target for PKA in vitro. The constrained configuration of the putative PKA site on the PP-1 holoenzyme may restrict its ability to be targeted by PKA.

Amino Acid Sequence↗
PubMed1976

Histochemical studies of the development of alkaline and acid phosphatase activities in the ovary and oviduct of the fowl (Gallus domesticus).

Alkaline and acid phosphatase activities were studied in the ovary and oviducts of pullets from the age of 2-32 weeks. Adult fowls were similarly studied. Alkaline phosphatase activity was present only in the glandular grooves and crypts of the immature oviducts. Alkaline phosphatase activity appeared at the pits of epithelial evaginations as glandular formation commenced. The young, non-secreting glands also showed the enzyme activity. But in the mature oviduct, alkaline phosphatase activity was confined to only the uterovaginal glands or sperm host glands and the epithelium of the vagina. In the ovary, alkaline phosphatase activity in the theca interna increased as the diameter of the follicles increased. Acid phosphatase activity was not present in the ovary, but in the oviduct, the enzyme activity was present in the uterine (shell gland) glands and in the uterovaginal epithelium and glands (sperm host glands). Alkaline phosphatase activity in the ovarian follicles and in the immature oviduct is thought to be related to histodifferentiation of these structures.

Acid Phosphatase↗
PubMed2003

Development of fluorescence-based selective assays for serine/threonine and tyrosine phosphatases.

A number of aromatic substrates were evaluated for their ability to detect tyrosine phosphatase and serine/threonine phosphatase activity. Results demonstrated that the fluorinated coumarin DiFMUP is the most sensitive substrate for detecting LAR and PP-2A activity. Using this substrate, selective high-throughput screening assays for serine/threonine and tyrosine phosphatases were developed. Specific inhibitor cocktails were added to each assay to limit the activity of other phosphatases. LAR, CD-45, and PTP-1B all rapidly hydrolyze DiFMUP in the tyrosine phosphatase assay. The activity of non-tyrosine phosphatases is less than 6% of the LAR activity. PP-1 and PP-2A are highly active in the serine/threonine phosphatase assay. Inhibition of LAR and PP-2A in these assays is demonstrated using known inhibitors. Both of these assays are sensitive, robust, kinetic assays that can be used to quantify enzyme activity.

Animals↗
PubMed1983

Impaired glycogenic substrate activation of glycogen synthase is associated with depressed synthase phosphatase activity in diabetic rat liver.

Glucose and gluconeogenic substrates promote the activation of hepatic glycogen synthase in vivo and in vitro; activation occurs as inactive glycogen synthase D is dephosphorylated to active glycogen synthase I by glycogen synthase phosphatase. Impairments of glycogen accumulation and glycogen synthase activation in diabetes have been attributed to decreased glycogen synthase phosphatase activity. To determine the role of glycogen synthase phosphatases associated with cytosol and smooth endoplasmic reticulum in the impairment of glycogen synthase activation, livers of normal and streptozotocin-diabetic fed rats were sampled by freeze-clamping before and after perfusion with a mixture of 25 mM glucose, 10 mM glutamine, 4 mM lactate, and 1 mM pyruvate. Perfusion induced activation of glycogen synthase in normal rats, but activation was reduced in the diabetic rats in proportion to the severity of insulin deficiency (r = 0.72, P less than 0.0001). There was also a close correlation between insulin levels and glycogen synthase phosphatase activities of both cytosol (r = 0.76, P less than 0.0001) and SER (r = 0.71, P less than 0.0001) fractions. In contrast, glycogen phosphorylase phosphatase activity and inactivation of glycogen phosphorylase during perfusion were normal in the diabetic livers. This is the first demonstration that glycogen synthase phosphatase activities in both soluble and SER fractions of liver cells are closely related to circulating insulin levels, and that the impairment of glycogen synthesis in diabetes may result from deficient glycogen synthase phosphatase activity in both cell compartments.

Animals↗
PubMedDate not supplied

Abnormal serum alkaline and acid phosphatase isoenzymes in female breast cancer patients.

Serum total, different isoforms of both alkaline and acid phosphatases, liver function enzymes, calcium, inorganic phosphate, heamatocrit, white blood cells and platelet counts were determined in 50 female patients suffering from breast cancer. The serum total alkaline and total acid phosphatases within the breast cancer group were variable with significant elevation of both enzymes compared with the corresponding control values. The activities of alanine and aspartate transferases were higher than the control values, while the decreases in serum albumin and heamatocrit were statistically significant. In the breast cancer patients, the increases in the activities of both heat and urea labile alkaline phosphatases were significant. Similarly, in the patients, the tartrate-labile acid phosphatases activity was significantly elevated while the difference in tartrate resistant activity was not significant. In 9 patients (18%), both total alkaline and acid phosphatases were excessively raised when compared with the control. The increased activities of urea-labile and heat-labile alkaline phosphatases as well as tartrate-resistant acid phosphatases are suggestive of increased activities of osteoclast and osteoblasts associated with bone metastasis. A possible diagnostic importance of this observation deserves further investigation, using monoclonal antibody techniques.

Acid Phosphatase↗
PubMed2001

Regulation of thromboxane receptor (TP) phosphorylation by protein phosphatase 1 (PP1) and PP2A.

To investigate the protein phosphatases that dephosphorylate TP, human embryonic kidney cells (HEK293 cells) stably transfected with 12CA5-tagged TP were treated with TP agonist, washed, and then allowed to recover in the presence or absence of the cell-permeable PP1 and PP2A inhibitors calyculin or okadaic acid (OKA). After recovery, cells were rechallenged with TP agonist and TP responsiveness was assessed by measuring inositol trisphosphate generation. TP responsiveness recovered over a 20-min time period. Recovery of TP responsiveness was inhibited by calyculin and OKA and was associated with dephosphorylation of receptor proteins. To further identify the TP phosphatase, TP phosphorylated in the intact cell were isolated by immunoprecipitation and were used as substrate for protein phosphatases prepared from HEK293 cells. TP were dephosphorylated by whole-cell homogenates. Dephosphorylation of TP was completely inhibited by the PP1 and PP2A inhibitors calyculin and microcystin-LR, suggesting that the decrease in TP phosphorylation was not due to receptor degradation. TP phosphatase activity was partially blocked by 1) inhibitor 2, a specific protein inhibitor of PP1; and 2) OKA at concentrations (1 nM) that specifically inhibit PP2A. TP phosphatase activity did not have an absolute requirement for divalent cations and was found primarily in cytosolic fractions of the cell. These data suggest that PP1- and PP2A-like protein phosphatases dephosphorylate TP. By regulating the phosphorylation state of TP, protein phosphatases may modulate tissue responsiveness to thromboxane.

Cations↗
PubMed2001

Induction of tumor specific cytotoxic T lymphocytes in prostate cancer using prostatic acid phosphatase derived HLA-A2402 binding peptide.

PURPOSE: Human prostatic acid phosphatase is a prostate specific differentiation antigen. Prostatic acid phosphatase levels increase in the serum of patients with prostate cancer and its peptide from positions 299 to 307 (PAP 299-307) is recognized by HLA-A2 restricted cytotoxic T lymphocytes. We investigated whether HLA-A2402 binding prostatic acid phosphatase derived peptides induce HLA-A2402 restricted, tumor specific cytotoxic T lymphocytes from the peripheral blood mononuclear cells of patients with prostate cancer. MATERIALS AND METHODS: Peptide binding activity was measured with RMA-S-A*A2402 cell lines and flow cytometry. Cytotoxic T-lymphocyte activity of the peripheral blood mononuclear cells of patients with prostate cancer and healthy donors was measured by interferon-gamma and (51)creatinine release assays. Prostatic acid phosphatase expression in the tumor cell lines at the messenger RNA and protein levels was investigated by reverse transcriptase-polymerase chain reaction and immunohistochemical analysis, respectively. RESULTS: An HLA-A2402 binding, prostatic acid phosphatase derived peptide consisting of the prostatic acid phosphatase amino acid sequence from positions 213 to 221 (PAP 213-221, LYCESVHNF) showed the ability to induce HLA-A2402 restricted and tumor specific cytotoxic T lymphocytes, which are cytoxic to prostatic acid phosphatase positive tumor cells from the peripheral blood mononuclear cells of patients with prostate cancer. CONCLUSIONS: PAP 213-221 may be appropriate as a cancer vaccine for specific immunotherapy in patients with HLA-A2402 positive prostate cancer.

Acid Phosphatase↗
PubMedDate not supplied

[Phosphatase activity in bone tissue and blood serum during 90-day hypokinesia].

Activities of alkaline and acid phosphatases in femoral epiphysis and diaphysis and those of alkaline phosphatase in the serum of rats that were exposed to a 3-month hypokinesia were measured. Phasic changes in the phosphatase activities were found in bone tissue. During the beginning of the hypokinetic experiment activities of both enzymes decreased as compared with the controls, the decrease of alkaline phosphatase being more significant. After the stress period activities of both phosphatases increased (especially of acid phosphatase in diaphysis) and by the end of the experiment were higher than the level of the enzyme activity in control rats. The activity of alkaline phosphatase in the serum varied in parallel with the enzyme activity in bones. The results give evidence for significant metabolic changes in the bone tissue during hypokinesia which lead to predominant resorption processes.

Acid Phosphatase↗
PubMed1992

The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei.

Nuclei from bovine thymus contain a high level of partially latent protein phosphatase 1 (PP-1). More than 90% of this PP-1 is associated with the insoluble chromatin/matrix fraction and can be extracted with 0.3 M NaCl. The salt extract also contains three heat- and acid-stable inhibitory proteins of PP-1 that can be resolved on Mono Q. We have purified two of these nuclear inhibitors of PP-1 (NIPP-1a and NIPP-1b) until homogeneity. They are acidic proteins (pI = 4.4) with a molecular mass of 18 kDa (NIPP-1a) and 16 kDa (NIPP-1b) on SDS-PAGE. Judged from the larger molecular mass that was deduced from gel filtration (35 kDa), NIPP-1a and NIPP-1b appear to be asymmetric or dimeric proteins. The nuclear inhibitors totally inhibited the phosphorylase phosphatase activity of PP-1, but even at a 250-fold higher concentration they did not affect the activities of the other major serine/threonine protein phosphatases (PP-2A, PP-2B, and PP-2C). NIPP-1a and NIPP-1b inhibited the catalytic subunit of PP-1 with an extrapolated Ki of about 1 pM, which is some three orders of magnitude better than the cytoplasmic proteins inhibitor 1/DARPP-32 and modulator. The nuclear inhibitors were not inactivated by incubation with protein phosphatases that inactivate inhibitor 1 and DARPP-32. Unlike modulator, they were not able to convert the catalytic subunit of PP-1 into a MgATP-dependent form. Remarkably, the extent of inhibition of PP-1 by NIPP-1b depended on the nature of the substrate. The phosphorylase phosphatase and casein phosphatase activities of PP-1 were completely blocked by NIPP-1b, whereas the dephosphorylation of basic proteins was either not at all inhibited (histone IIA) or only partially (myelin basic protein). These data may indicate that the acidic NIPP-1b is inactivated through complexation by basic proteins. Indeed, nonphosphorylated histone IIA antagonized the inhibitory effect of NIPP-1b on the casein phosphatase activity of PP-1. Our data show that the nucleus contains specific and potent inhibitory proteins of PP-1 that differ from earlier described cytoplasmic inhibitors. We suggest that these novel proteins may control the activity of nuclear PP-1 on its natural substrate(s).

Animals↗
PubMed1985

Phosphotyrosine phosphatase activity in human placenta.

A phosphotyrosine phosphatase was enriched 9-fold from human placenta homogenates using ammonium sulfate fractionation and chromatographies on P-cellulose and Phenyl Sepharose. The enzyme preparation hydrolyzed phosphotyrosine, p-nitrophenyl phosphate, as well as phosphoenol-pyruvate. The enzyme was unstable, and its Km value for phosphotyrosine increased during the purification procedure. The optimum pH for phosphotyrosine was found to be pH 7.0. The phosphotyrosine phosphatase activity was completely inhibited at 2.6 mM Cu2+. Zn2+ was slightly inhibitory to the phosphatase activity. The effects of several inhibitors on the phosphotyrosine phosphatase activity were different from those on the p-nitrophenyl phosphatase activity. These results suggest that the phosphotyrosine phosphatase activity from human placenta is different from previously reported acid and alkaline phosphatases.

Cations, Divalent↗
PubMed1985

Identification of protein phosphatase 1 in synaptic junctions: dephosphorylation of endogenous calmodulin-dependent kinase II and synapse-enriched phosphoproteins.

A calcium/calmodulin-dependent protein kinase termed CaM-kinase II is a major component of synaptic junctions from forebrain and constitutes approximately 12% of total synaptic junction protein. CaM-kinase II phosphorylates at least seven polypeptides that are enriched in synaptic junctions, of which two represent the 50- and 60-kilodalton subunits of the protein kinase. In this report the nature of endogenous protein phosphatases which dephosphorylate each of the seven synaptic junction phosphoproteins was examined. Assays of synaptic junctions and other subcellular fractions from rat forebrain for type-1 and type-2 protein phosphatases revealed that protein phosphatase 1 (PrP-1) was specifically enriched in synaptic junctions with respect to cytosolic fractions. The activity of type-2 protein phosphatases was very low in synaptic junctions. Homogeneous PrP-1 from rabbit skeletal muscle was found to dephosphorylate each of the seven phosphoproteins in synaptic junctions. Inhibitors-1 and -2 were found to inhibit endogenous protein phosphatase activity by 70 to 80%. Since inhibitors-1 and -2 are specific inhibitors of PrP-1, these results indicate that this enzyme accounts for the majority of endogenous protein phosphatase activity in synaptic junctions. Approximately 15% of the protein phosphatase activity in synaptic junctions was type 2A, whereas PrP-2B and PrP-2C accounted for little, if any, of the activity toward endogenous or exogenous phosphoproteins. These results indicate that PrP-1 may be important in controlling the state of phosphorylation of synaptic junction proteins.

Animals↗
PubMed1986

Interaction of the 56,000-dalton phosphoprotein phosphatase from reticulocytes with regulin and inhibitor 2.

The interaction of divalent metal ions with a homogeneous 56,000-dalton phosphoprotein phosphatase isolated from rabbit reticulocytes was studied. The effects of the ions on enzymatic activity and on fluorescence from a 3-(4-maleimidylphenyl)-4-methyl-7-(diethylamino)coumarin derivative of the protein were compared. Enzymatic activity is dependent on Mn2+. The apparent association constant for Mn2+ is about 0.5 mM-1 as judged from enzymatic activity and from changes in fluorescence caused by binding of the metal ion; Ca2+ and Mg2+ do not affect enzymatic activity and appear not to bind tightly to the enzyme; however, Co2+, Fe2+, and Zn2+ bind to the protein and inhibit the Mn2+-activated enzyme. The 56,000-dalton phosphoprotein phosphatase was found to interact with regulin, a spectrin-associated protein also isolated from reticulocytes, and with skeletal muscle phosphatase inhibitor 2. The interaction was followed by changes in the enzymatic activity and by quenching of fluorescence from the coumarin derivative of the phosphatase. Homogeneous regulin (Mr approximately 230,000) increases the activity of the enzyme severalfold; this stimulation is Mn2+-dependent. Inhibitor 2 decreases enzyme activity but only if the two proteins are preincubated in the absence of Mn2+. Comparable differences in the effect of Mn2+ were also observed in parallel experiments in which changes in fluorescence from the coumarin-labeled 56,000-dalton phosphatase were measured. In these experiments, it was shown that Mn2+ enhances the interaction between regulin and the 56,000-dalton phosphatase, but inhibits the interaction between the phosphatase and inhibitor 2.

Animals↗
PubMed1986

Polyamine stimulation of protein phosphatase-2A from rat liver using a non-protein phosphoester substrate.

The polyamines, spermine and spermidine, activate a high molecular weight form of phosphorylase a phosphatase isolated from rat liver. This broad specificity protein phosphatase (type 2A) was partially purified, using both protein and non-protein phosphoester substrates. Spermine and spermidine activated isolated protein phosphatase-2A1 (apparent Mr 210,000) approximately 2-fold, when p-nitrophenyl phosphate (PNPP) was used as substrate. Freeze-thawing, which activated the phosphatase activity against a variety of phosphoprotein substrates, also increased the extent of stimulation of PNPP phosphatase activity by spermine (8 to 9-fold with Ka of 93 microM) and spermidine (6 to 7-fold with Ka 280 microM). Kinetic analysis indicated that the activation of phosphatase by polyamines was accomplished by an increase in Vmax of the enzyme, by a mechanism independent of that achieved by other cations. The data indicate that polyamines, at physiological concentrations, can activate a form of protein phosphatase widely distributed in mammalian tissues, and thereby influence cellular protein phosphorylation.

Animals↗
PubMedDate not supplied

[Alterations in acid and alkaline phosphatase activity in some steroid-producing organs of rats in autolysis].

Alterations in activity of acid and alkaline phosphatases as well as in concentration of inorganic phosphate were studied in tissue and homogenates of adrenal glands and testicles of rats within 48 hrs of the postmortal autolysis. During the autolysis acid phosphatase of homogenate and tissue of adrenal glands as well as alkaline phosphatase from the gland were more stable than acid and alkaline phosphatases from testicles. Activities of acid and alkaline phosphatases decreased gradually in homogenate and tissue of testicles during autolysis. Within the first day of autolysis distinct inhibition of alkaline phosphatase was also observed in the homogenate of testicles and adrenal glands. An increase in amount of inorganic phosphate in tissue and homogenate of adrenal gland and in tissue of testicles did not depend on alterations in activity of the phosphatases on autolysis. Prehomogenization of these tissues altered markedly the enzymatic activity both in adrenal glands and in testicles.

Acid Phosphatase↗