Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Gene/Protein
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Target Concepts:
Gene/Protein
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Enzyme
Compound
Query: EC:3.1.3.1 (
alkaline phosphatase
)
47,916
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Testicular estrogen receptors were measured in the presence of phosphatase inhibitors, molybdate (MoO4=), wolframate (WO4=) and fluoride (F-), under different experimental conditions. At 0-4 degrees C, MoO4= was able to partially replace the stabilizing action of dithiothreitol (DTT) on cytosolic estrogen binding activity, suggesting a protective effect on reduced sulfhydryl groups. At 25 degrees C in the presence of DTT, the effect of MoO4= was observed in homogenates and low speed supernatants, being uneffective in cytosol. A possible mechanism of action through inhibition of phosphatase activity was supported by the use of WO4=.
Acid phosphatase
activity was inhibited in the presence of these agents, whereas
alkaline phosphatase
was unaffected. The addition of MoO4= also caused a significant inhibition of proteolytic activity. These results suggest that MoO4= would stabilize testicular estrogen binding activity through, at least, three mechanisms: 1) protection of reduced sulfhydryl groups; 2) inhibition of acid phosphatase, and 3) inhibition of proteolytic activity.
...
PMID:Effect of phosphatase inhibitors on estrogen receptors in the rat testis. 282 32
Soybean acid phosphatase (
orthophosphoric-monoester phosphohydrolase
, EC 3.1.3.2) was completely separated from phytase (EC 3.1.3.8) isolated from cotyledons of germinating seeds and purified to homogeneity. A four-step purification regimen consisting of ammonium sulfate fractionation, and ion-exchange, affinity, and chromatofocusing gel chromatographies was employed to achieve a homogeneous preparation.
Acid phosphatase
activity appeared as a major band of the three forms of acid phosphatase identified on native gels. The purified enzyme had a molecular weight of 53,000 when electrophoresed on 8% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and a molecular weight of 53,000 from its mobility in a Fracto-gel TSK HW-50F gel permeation column. The molar extinction coefficient of the enzyme at 278 nm was estimated to be 4.2 X 10(4) M-1 cm-1. The isoelectric point of the protein, as revealed by chromatofocusing, was about 6.7. The optimal pH for activity, like other plant acid phosphatases, was 5.0. While the enzyme failed to accommodate phytate as a substrate, the enzyme did exhibit a broad substrate selectivity. The affinity of the enzyme for p-nitrophenyl phosphate was high (Km = 70 microM), and activity was competitively inhibited by orthophosphate (Ki = 280 microM). The estimated catalytic turnover number (Kcat) of the enzyme for p-nitrophenyl phosphate was about 430 per second. Although the purified enzyme was stable at 0 degrees C and exhibited maximum catalytic activity at 60 degrees C, thermal inactivation studies indicated that the enzyme lost 100% activity after treatment at 68 degrees C for 10 min.
...
PMID:Purification and characterization of acid phosphatase from cotyledons of germinating soybean seeds. 282 34
Thiamine pyrophosphatase was demonstrated in the Golgi complex and acid phosphatase in the GERL of acinar cells of submandibular and parotid glands and were previously demonstrated in cells of intercalary ducts. Thiamine pyrophosphatase was also demonstrated in the Golgi complex of cells of striated and excretory ducts and myoepithelial cells.
Acid phosphatase
was also demonstrated in lysosomes. Alkaline phosphatase was rarely demonstrated light microscopically at luminal surfaces of striated and excretory ducts and electron microscopically in luminal vesicles in cells of striated ducts. The demonstration of the phosphatases in Golgi complexes and GERLs indicates that investigations on these structures in experimental animals are relevant to human salivary glands and supports the opinion that ductal cells as well as acinar cells secrete organic material. The presence of
alkaline phosphatase
at luminal surfaces of striated and excretory ducts suggests that resorption as well as secretion may occur in them.
...
PMID:Ultrastructural phosphatase histochemistry of submandibular and parotid salivary glands of man. 283 35
Twenty patients with stage D2 prostatic carcinoma were treated for up to 18 months with D-Trp-6-LH-RH. Results of more than 3 months of treatment on these 20 patients are reported. The analog was given SC once daily at a dose of 1,000 micrograms/day. All patients had bone pain and high levels of acid and
alkaline phosphatase
. After the first week of D-Trp-6-LH-RH administration, major decreases in bone pain and reversal of the signs of prostatism were observed.
Acid phosphatase
gradually fell, achieving normal values after 12 weeks. Initial plasma testosterone was within normal limits, but during treatment with D-Trp-6-LH-RH it fell to castration levels. Resting values of PRL, GH, TSH, and cortisol did not show significant changes. After TRH, TSH increased in five patients, but five did not respond. However, at 2 and 4 months, all patients released TSH in response to TRH. Two patients died during the treatment with D-Trp-6-LH-RH despite initial subjective responses and decreases in testosterone levels. The rise in acid phosphatase levels in these two patients was accompanied by a general deterioration, suggesting that they had androgen-independent cancer. One patient who developed progressive hepatic, bone, and pulmonary metastases in spite of previous orchiectomy was also treated with the analog. Three months later his acid phosphatase levels were within normal values, and partial regression of metastases was observed. These results demonstrate that D-Trp-6-LH-RH and other LH-RH agonists can be used as an effective endocrine therapy for advanced prostate carcinoma, thereby avoiding the side effects of estrogens or the psychological impact of surgical castration.
...
PMID:Treatment of advanced prostatic carcinoma with D-Trp-6-LH-RH. 293 92
The cytochemical localization of enzymatic activity by means of backscattered electron imaging (BEI) is reviewed and the application of BEI to changes in acid phosphatase and ATPase distribution during physiological (programmed) cell death in Heliothis midgut is explored. Programmed cell death entails the release of nascent free acid phosphatase as extracisternal hydrolase. This shift can readily be detected by means of the atomic number contrast imparted by BEI of the lead phosphatase reaction product, thus enabling the distribution of dying cells to be mapped. BEI is particularly useful in this context as it allows the examination of bulk specimens at low magnification. Death of cells is also accompanied by a collapse in ATPase activity which shows up as cytochemically negative areas in the X-ray microscope and by means of BEI.
Acid phosphatase
in normal cells is localized in the apical microvilli and lysosomes. Senescent or dying cells, however, clearly show a basally situated free hydrolase which migrates throughout the cell. Parallel TEM results confirm that this enzyme is ribosomal and extracisternal rather than lysosomal in origin. ATPase activity is largely limited to the apical microvilli, although there is some activity associated with the basal plasma membranes. The apical ATPase, however is partially resistant to ouabain. Young and mature cells are positive although in the latter case some microvilli may be lost as the cells acquire a negative cap or dome. Inhibition by bromotetramizole indicates that apical activity is not to any significant extent contributed to by
alkaline phosphatase
. Degenerate or dead cells are negative and can be seen as a mozaic of "black patches" among normal cells when imaged by means of BEI or X-ray microscopy.
...
PMID:The use of backscattered electron imaging, X-ray microanalysis and X-ray microscopy in demonstrating physiological cell death. 297 76
The relationships among phosphorus phase feeding, egg shell quality, and the activities and concentrations of several enzymes and minerals in the uterine and isthmus mucosae of hens at the time of oviposition were investigated. During the first 8 months of production (Phase 1), layer diets contained .3, .5, or .7% available phosphorus. Between 9 and 12 months of production (Phase 2), dietary available phosphorus was either increased or decreased by .2% phosphorus, or was left unchanged. No significant differences due to Phase 1 diets were demonstrated for hard-shelled (HS), soft-shelled (SS), or shell-less (SL) egg production, livability, egg weight, or specific gravity. Phase 2 diets had no significant effect on SS or SL egg production, livability, or egg specific gravity; however, decreasing dietary phosphorus reduced egg weight. Levels as high as .9% had no effect on specific gravity or HS egg production, while .1% dietary phosphorus was detrimental to HS egg production and feed consumption. No significant differences due to dietary available phosphorus or egg type (SS vs. HS) were demonstrated for uterine or isthmus mucosal enzyme activities or mineral contents, with one exception. Higher inorganic phosphorus concentrations were found in the uterus of HS egg layers when compared to levels in the uterus of SS egg layers and the isthmus of HS and SS egg layers.
Acid phosphatase
and carbonic anhydrase activities, and total calcium levels were significantly higher in the isthmus than the uterus, while
alkaline phosphatase
and pyrophosphatase activities, and inorganic phosphorus levels were significantly higher in the uterus than the isthmus.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Phosphorus phase feeding and uterine and isthmus mucosal enzymes and minerals in relation to soft-shelled and shell-less egg production. 299 45
We applied cytochemical procedures to demonstrate the presence of acid and
alkaline phosphatase
in the visceral yolk-sac endoderm of rats using frozen, aldehyde-fixed tissue with cerium as the capture agent. This procedure allowed more detailed topochemical localization than was possible using unfrozen tissue or with lead as the capture agent.
Acid phosphatase
was found to be present in lysosomes as well as in a small number of apical canaliculi, which are thought to be recycling structures of the cell membranes in endodermal cells. Reaction products of
alkaline phosphatase
were observed on the outer surface of apical, lateral, and basal cell membranes. In addition, some apical vacuoles contained
alkaline phosphatase
, and more apical canaliculi were positive for
alkaline phosphatase
than for acid phosphatase. However, most of the apical canaliculi were negative for both enzymes. It is suggested that acid and
alkaline phosphatase
are taken up by different numbers of apical canaliculi during the detachment of apical canaliculi from lysosomes and resorption vacuoles.
...
PMID:Cytochemical demonstration of phosphatases in membrane-recycling structures of endodermal cells. 303 36
Percoll density gradient centrifugation was used for isolating large quantities of bradyzoites of Sarcocystis suicanis, which were used for enzymatic analysis. Crude extracts of bradyzoites contained activities suggestive of several acid hydrolases. Levels of acid and
alkaline phosphatase
were higher than those of beta-N-acetylhexosaminidase and beta-galactosidase.
Acid phosphatase
was purified 156-fold with an overall recovery of 54% using DEAE-Sepharose 4B and Sephadex G-200 chromatography. The partially purified enzyme was not a glycoprotein and had a molecular weight of approximately 170,000. The enzyme was markedly inhibited by Cu++, Hg++, and iodoacetamide, suggesting the presence of a sulfhydryl group. Sodium tartrate caused strong inhibition of the enzyme. The acid phosphatase of S. suicanis appears to be a unique enzyme that cannot be classified under high or low molecular weight acid phosphatases of widely diverse origin.
...
PMID:Studies on the enzymes of Sarcocystis suicanis: purification and characterization of an acid phosphatase. 311 63
The isolated brush border membrane of the tapeworm, Hymenolepis diminuta, hydrolyzes p-nitrophenyl phosphate over a broad pH range.
Acid phosphatase
activity (pH optimum at 4.0) is inhibited specifically by sodium dodecyl sulfate (SDS) and NaF, while the
alkaline phosphatase
activity (pH optimum at 8.8) is inhibited specifically by levamisole, 2-mercaptoethanol, and ethylenediaminetetra-acetate (EDTA). These two phosphatase activities are further differentiated in that (1) there is a rapid decrease in
alkaline phosphatase
activity when the membrane preparation is incubated at pH 4.0, while there is little loss of acid phosphatase activity, and (2) the
alkaline phosphatase
activity is solubilized with no loss of activity when the membrane is treated with Triton X-100, while such treatment causes a significant loss of acid phosphatase activity. Both activities are nonspecific and hydrolyze a variety of phosphorylated compounds, but the relative activities of the two phosphatases against these substrates vary significantly.
...
PMID:Acid phosphatase activity in the isolated brush border membrane of the tapeworm, Hymenolepis diminuta: partial characterization and differentiation from the alkaline phosphatase activity. 341 89
A histological and histochemical study of ingested food material, energy stores and enzymes in the monogenean Pseudodactylogyrus anguillae, parasitizing the gills of the European eel (Anguilla anguilla) is presented. It was found that mucus, epithelial cells and blood from the gills were ingested. Glycogen deposits were small and primarily located in the parenchyma and to a minor extent in the vitellariae. Numerous globules of neutral lipids were found in the vitellariae. A marked esterase activity was found in the gut and a less marked activity in the vitellariae.
Acid phosphatase
activity was found throughout the body whereas
alkaline phosphatase
and leucine-amino-peptidase were not detected. Marked activity of succinate dehydrogenase and NADH-diaphorase was found in all cells, indicating a predominantly aerobic metabolism in this monogenean.
...
PMID:The nutrition of the gill parasitic monogenean Pseudodactylogyrus anguillae. 342 77
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