Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acid phosphatase II (AP II) was isolated from the cell-free extract of Pichia guilliermondii Wickerham ATCC 9058 and partially purified. The enzyme is a non-specific phosphomonoesterase. It hydrolyzes p-nitrohenyl-phophate (NPP), beta-glycerophosphate, glucose-6-phosphate, guanosine-5'-monophosphate, adenosine-5'-monophosphate, cytidine-5'-monophosphate, uridine-5'-monophosphate, alpha-naphtylphosphate, FMN. The order of the substrates corresponds to the degree of their hydrolysis decrease. The Michaelis constant of the enzyme was 1.4-10-3 M for NPP as a substrate, pH optimum was 5.5 and temperature optimum-40C. AP II was strongly inhibited by MoO4-2, F-, inorganic phosphate, Cu2+ and Be2+. The activity of the enzyme in the yeast cells does not change noticeably during growth on media with low and high iron content.
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PMID:[Study of acid phosphatase II from Pichia guilliermondii yeasts]. 0 63

Lysed granule fraction was prepared from splenic adherent cells from 0-day-old to 2-month-old chickens and was examined antibacterial activity to Salmonella pullorum and Salmonella sentfenberg. The activity of lysed granule fraction from 2-month-old chickens was exhibited at pH 5.0 but not exhibited at pH 6.0 or 7.0 to both serotypes of Salmonella. At pH 5.0, lysed granule fraction from 0-day-old chickens revealed little antibacterial activity to S. pullorum but the activity increased with increasing age. At 240 min of incubation, 60% and 95% of S. pullorum were inactivated in lysed granule fractions from 7-day-old and 2-month-old chickens, respectively. High antibacterial activity to S. senftenberg was observed in lysed granule fraction from 2-month-old chickens in which 99.6% of the bacteria was inactivated during 240 min; In lysed granule fractions from 0-day old and 7-day-old chickens, 90% of S. senftenberg was inactivated during 60 min but the number of bacteria increased conversely after incubation for 240 min. Changes in enzymatic activities of 4 enzymes in the lysed granule fractions from various ages of chickens were examined. beta-Glucronidase increased statistically significantly to 2.4 and 7.6 times from 0-day-old to 7-day-old and 2-month-old chickens, respectively. Acid phosphatase and alkaline phosphatase increased slightly but not significantly different, and enzymatic activity of myeloperoxidase was scarcely detected.
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PMID:Age-dependent resistance of chicken of Salmonella in vitro: antibacterial activity of lysed granule fraction of splenic adherent cells. 1 89

Acid and alkaline phosphatase activity has been localized in the cells of the sterile septae of starved and fed anthozoa. Acid phosphatase is present in lysosomes, in Golgi cisternae and old phagosomes of starved animals. In fed animals, the reaction is more intense and the number of lysosomes is increased. New phagosomes are loaded with lead phosphate. In starved animals, the alkaline phosphatase activity has been observed on the plasma membranes and in the old phagosomes.
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PMID:[Ultrastructural localization of acid and alkaline phosphatases in sterile septae of the anthozoa Pachycerianthus fimbriatus (author's transl)]. 2 64

We prepared the 5'- and 3'-O-phosphorothioate esters of the antitumor agent O2 : 2'-anhydro-1-beta-D-arabinosylcytosine. We also included in this study esters of 2'-thio-2'-deoxycytidine, namely, 2'-S-dCyd-2' : 3'-P, 2'-S-dCyd-2'-P, and 2'-S-dCyd-3'-P, along with natural nucleotides. These compounds were subjected to the action of Escherichia coli alkaline phosphatase, potato acid phosphatase, and bovine pancreatic ribonuclease A. The data were analyzed by Lineweaver-Burk plots to obtain Km and KI values. Only 2'-S-dCyd-2'-P was a substrate for alkaline phosphatase; the anhydro-araCyt phosphorothioates were good competitive inhibitors, while 2'-S-dCyd-3'-P did not associate with the enzyme. Acid phosphatase hydrolyzed all four monoesters investigated, including the S-phosphorothioate. The cyclic phosphorothioate, 2'-S-dCyd-2' : 3'-P was neither hydrolyzed by, nor associated with, ribonuclease A. ORD spectroscopy was also used in an attempt to relate the structural features of analogs to the peculiarity of their hydrolysis.
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PMID:The enzymatic hydrolysis of the phosphate ester bond in some thionucleotides. 8 87

Various histochemical and histological techniques were used to study the melanin and dopa-positive cell distribution in the skin of some tropical and temperate breeds of cattle in Nigeria. Melanin pigments were concentrated in the basal and lower spinous layers of the epidermis and in the hair cortex, follicle sheaths and papillae of the various breeds. In the White Fulani and N'Dama breeds, melanin pigments were however found in all layers of the epidermis. Dopa-positive cells (melanocytes) were observed in the epidermis, dermis and hair follicles; the distribution pattern varied among breeds, being copiously disposed in the basal epidermis and papillary dermis in the White Fulani and Muturu and, except in areas of thick epidermal ridges, scanty in the epidermis and dermis of the Friesian and N'Dama. Mast cell distribution pattern in the various breeds was similar to that of the dopa-positive cells. Peroxidase-positive cells were present in the basal epidermis and upper dermis of the Muturu, widespread in the subepidermal layer of the N'Dama and very scanty in the dermis of the White Fulani and Friesian. Acid phosphatase activity was intense in the granular layer of the Muturu and N'Dama breeds and also in the papillary dermis and hair follicles, whereas alkaline phosphatase-positive dendritic cells, and 'clear' cells were also observed in the basal and upper epidermis.
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PMID:Melanin and dopa-positive cells in the skin of tropical cattle. 8 2

The study deals with the distribution of acid and alkaline phosphatases, ATPase, 5-nucleotidase, nonspecific esterase, specific cholinesterase, and beta-galactosidase in the diencephalon of the frog. The highlights of the present study are the following: i) Acid phosphatase is present in all the neurons, whereas the tracts and commissures are completely negative. ii) Most of the tracts and commissures are positive for 5-nucleotidase. This confirms the author's previous findings that the tracts and commissures of all the areas of frog brain are intensely positive for 5-nucleotidase. iii) beta-galactosidase activity in the nuclei of the diencephalon is either mild or completely absent, whereas the commissures and tracts show positive activity. iv) Habenulothalamic connections are intensely positive for specific cholinesterase and non-specific esterase, moderately positive for beta-galactosidase and completely negative for other enzymes. v) The epiphysis (pineal organ) shows intense reaction for adenosine triphosphatase, acid phosphatase, and 5-nucleotidase and moderate reaction for alkaline phosphatase and non-specific esterase. In contrast to the above enzymes, the specific cholinesterase and beta-galactosidase are completely missing. vi) Lateral forebrain bundles are completely negative for all the enzymes except alkaline phosphatase and beta-galactosidase. The distribution of these enzymes has been correlated with the functional aspects of various nuclei, tracts, and commissures of the diencephalon of the frog.
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PMID:The chemoarchitectonics of the diencephalon of frog (Rana tigrina). 15 81

The enzymatic changes in chronic hypertrophic rhinitis were studied in 14 patients. The cholinesterase content was increased in the subepithelium and stroma, denoting parasympathetic hyperactivity. Acid phosphatase was increased in the epithelium, subepithelium and around the glands, indicating increased shedding and phagocytic activity. Succinic dehydrogenase, alkaline phosphatase and alpha-esterase were increased in the mucous glands, denoting increase secretory activity, hence increased natural defence mechanism of the nasal mucosa.
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PMID:Chronic non-allergic hypertrophic rhinitis. A histochemical study. 15 75

One theory of the development of cleft palate in rats involves the action of lysosomal enzymes secreted by epithelial cells at the time of fusion of the palatal shelves. To test this theory we studied the biochemistry of the palates of fetal rats daily between days 14 and 19 (from 3 days before to 3 days after palate closure). Triamcinolone was administered once im on gestation day 14 to Wistar rats; 0.5 mg/kg body weight produced approximately 50% cleft palates. Pooled control palatal tissue was compared with pooled experimental tissue; that from fetuses with clefts being pooled separately from those not affected. Acid phosphatase and beta-glucuronidase were assayed. Concentration vs. time curves for both enzymes were very similar. Prior to the time of palate closure both enzymes were present in low concentration. Between days 16 and 17, the normal time of closure, there was an abrupt increased in enzyme concentration, with experimental tissue showing a significant elevation over control tissue on days 17 and 18. Alkaline phosphatase was also present in small amounts before closure and significantly higher in control tissue on day 17. Protein was depressed in palates having clefts on day 17; thus the ratio of enzyme activities to protein synthesis was significantly elevated at a critical time. Unaffected experimental palates had a normal ratio. These results suggest imbalanced acid phosphatase, beta-glucuronidase, and alkaline phosphatase activity compared with protein synthesis at the time of palate closure following triamcinolone in rats.
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PMID:Tissue phosphatase changes following triamcinolone associated with cleft palate in rats. 16 57

The purpose of this study was to try to differentiate histochemically between the various enzymes which may catalyze the hydrolysis of ATP in developing rat dental tissues. Freeze cut and freeze dried sections of molar and incisor teeth were incubated in lead capture-based media at pH 5.0, 7.2 or 9.4 with one of the following substrates: beta-glycerophosphate, AMP, ADP, ATP, AMP-PNP and tetrasodium pyrophosphate. To establish the enzymatic nature of the hydrolysis parallel sections were incubated after prior fixation in either formaldehyde or glutaraldehyde. By comparing the enzymatic stainings obtained with the various substrates and at the different pH:s, it was concluded that ATP can be visibly hydrolyzed in rat dental tissues by alkaline phosphatase (stratum intermedium, apical part of maturation ameloblasts, basal part of all ameloblasts, odontoblasts and subodontoblastic layer), specific ATPase (apical and basal parts of secretory ameloblasts) and ATP pyrophosphatase and/or adenylate cyclase (stratum intermedium, odontoblasts). Acid phosphatase, specific ADPase, 5'-nucleotidase, inorganic pyrophosphatase, 3':5'-cyclic-AMP-phosphodiesterase and adenylate kinase on the other hand, seem not to be engaged in the ATP hydrolysis to such a degree as to complicate the interpretation of the histochemical staining. The alkaline phosphatase part of the ATP hydrolysis appeared to be rather insensitive to aldehyde fixation, while the hydrolysis effected by specific ATPase and ATP pyrophosphatase and/or adenylate cyclase was extinguished after fixation with formaldehyde for 4 h or glutaraldehyde for 10 min.
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PMID:Adenosine triphosphate hydrolysis in rat dental tissues. A histochemical study to differentiate the enzymes involved. 18 60

1. The biochemical development and histochemical localisation of phosphomonoesterases in the testes of prepuberal chicks have been studied. 2. Maximum acid phosphatase activity was observed at 12 weeks with a decrease in enzyme activity after this age, whereas alkaline phosphatase activity fluctuated with age. 3. Acid phosphatase activity in chicks was similar to that of the cockerel in being tartarate-insensitive. 4. There was a low level of significant correlation between acid phosphatase activity and testes weight. 5. Both alkaline and acid phosphatase activities were observed in the basement membrane of the seminiferous tubules, and acid phosphatase activity also in the various spermatogenic elements. 6. The results suggest that acid phosphatase is more involved in spermatogenesis, and more widely distributed than alkaline phosphatase in testicular tissue during testicular development.
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PMID:The development of phosphomonesterases in the testes of prepuberal chicks. 18 28


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