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)

The activity of phosphohydrolase (acid, alkaline, pyrophosphatase) was studied in two strains of Pseudomonas maltophilia: VCM-B-591 and SSE-B-715. The activity of these enzyme systems in these strains was found to be much higher than in other Pseudomonas species, viz. Ps. aeruginosa VCM-B-889, Ps. fluorescens VCM-B-553, Ps. geniculata SSE-B-338, and in E. coli B. The phosphohydrolase activity of Ps. maltophilia varied depending on the growth phase of the culture. The highest activity of acid phosphatase was registered in the middle of the exponential phase for the strain VCM-B-591 and at the beginning of this phase for the strain SSE-B-715. The activity of alkaline phosphatase was maximal, for both of the strains VCM-B-591 and SSE-B-715, at the beginning of the logarithimic growth phase. The pyrophosphatase activity of the two strains had "two peaks" at the beginning and by the end of the logarithmic phase of growth. Incubation of Ps. maltophilia cells in media without orthophosphate did not result in an increase of their phosphohydrolase activity.
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PMID:[Phosphohydrolase activity of Pseudomonas maltophilia]. 23 Nov 88

Fractions composed primarily of cells (Fraction I), membrane fragments (Fraction II) and matrix vesicles (Fraction III) were isolated from chick epiphyseal cartilage. The characteristics of the alkaline phosphatase (EC 3.1.3.1), pyrophosphatase (EC 3.6.1.1) and ATPase (EC 3.6.1.3) activities in the matrix vesicle fraction were studied in detail. Mg-2-+ was not absolutely essential to any of the activities, but at low levels was stimulatory in all cases. Higher concentrations inhibited both pyrophosphatase and ATPase activities. Both the stimulatory and inhibitory effects were pH-dependent. Ca-2-+ stimulated all activities weakly in the absence of Mg-2-+. However, when Mg-2-+ was present, Ca-2-+ was slightly inhibitory. Thus, none of the activities appear to have a requirement for Ca-2-+, and hence would not seem to be involved with active Ca-2-+ transport in the typical manner. The distribution of alkaline phosphatase, pyrophosphatase, and Mg-2-+ ATPase activities among the various cartilage fractions was identical, and concentrated primarily in the matrix vesicles. Conversely, the highest level of (Na-+ + K-+)-ATPase activity was found in the cell fraction. All activites showed nearly identical sensitivities to levamisole (4 - 10-3 M) which caused nearly complete inhibition of alkaline phosphatase and pyrophosphatase. About 10-15% of the ATPase activity was levamisole-insensitive. The data are consistent with the concept that the Mg-2-+-ATPase and pyrophosphatase activities of matrix vesicles stem from one enzyme, namely, alkaline phosphatase.
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PMID:Studies on matrix vesicles isolated from chick epiphyseal cartilage. Association of pyrophosphatase and ATPase activities with alkaline phosphatase. 23 58

Callus calcifying cartilage alkaline phosphatase was resolved by DEAE-cellulose column chromatography into two distinct phsophatase activities. The phosphatase activity which was eluted first from the column, (phosphatase I), was active towards a variety of phosphate esters, sodium pyrophosphatase and several linear polyphosphates, while the second phosphatase activity , (phosphatase II), was active toward simple phosphate esters but not towards sodium pyrophosphate and linear oligo or polyphosphates. All the phosphate esters, sodium pyrophosphate and polyphosphates at higher concentrations were inhibitory for phosphatase I. The modulating effects of magnesium, calcium, zinc and other phosphatase modulators have been investigated. Both phosphatases from callus calcifying cartilage were found to be substrates of neuraminidase with sialic acid as the product. Besides the difference in their specificity, the phosphatases were found to be immunologically different and to have different molecular weights, strong indication that they are different enzymes.
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PMID:Resolution, purification and characterization of the orthophosphate releasing activities from fracture callus calcifying cartilage. 23 99

Rats were injected with a single intravenous dose of aminonucleoside (AMN) and sacrificed 1-48 h later. The activity of several enzymes was assayed in the Golgi apparatus isolated from the liver. Galactosyltransferase activity showed little changes after the AMN, but both acid (EC 3.1.3.2) and alkaline phosphatase (EC 3.1.3.1) activities increased within the first hour and reached control levels only 5-24 h later. Thiamine pyrophosphatase and arylsulfatase A (EC 3.1.6.1) activities also increased and stayed at higher levels for the duration of the experiment. Arylsulfatase B (EC 3.1.6.1) activity decreased shortly after the AMN but later increased to above control levels. These findings support earlier results in which liver ultrastructural and biochemical changes were observed early before renal lesions and proteinuria.
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PMID:Early effects of aminonucleoside on enzymes in the Golgi apparatus of rat liver. 24 Apr 92

The paper deals with the histochemical and cytochemical distribution of thiamine pyrophosphatase (TPP-ase 3.6.1.) in the normal rat gastric mucosa using the method of NOVIKOFF and GOLDFISCHER (1961). In light microscopy, activity was demonstrated only in the GOLGI apparatus of the foveolar mucous cells; in the other specialized gastric mucosal cells no activity was established. At electron microscopic level, the reaction product was localized in the membranes of the cisternae of the GOLGI apparatus of foveolar mucous cells, undifferentiated neck cells, parietal cells, chief cells and in endocrine cells. The reaction product was not found in the endoplasmic reticulum of any of the above mentioned types of cells with the exception of parietal cells. The deposits of the reaction product in the cytoplasmic membrane, in the capillary endothelium and on the surface of the plasma membrane of foveolar mucous cells represents the sites of activity of alkaline phosphatase. The examination of the TPP-ase in the gastric mucosa inables us to estimate the activity of the GOLGI apparatus of gastric mucosal cells in the norm and in different pathological conditions connected with its changes.
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PMID:Histochemistry and cytochemistry of thiamine pyrophosphatase (TPP-ase 3.6.1.) in the rat gastric mucosa. 41 87

The effect of local irradiation of a 50-cm long intestinal segment outside the abdominal cavity in rabbits has been studied. The rabbits were killed at 12, 24, 48 and 72 hours after irradiation. Activities of succinate and lactate dehydrogenase, acid and alkaline phosphatase and thiamine pyrophosphatase were studied histochemically in the irradiated intestinal segment and in the part of the intestine remaining in the abdominal cavity. The same material was studied electron-microscopically. Changes in enterocytes of the intestinal crypts were observed mainly in the mitochondria and in the form of a chaotic distribution of endoplasmic membranes and densely scattered ribosomes. In intestinal crypt cells, irradiation was followed by a depression in the activities of succinate and lactate dehydrogenases and alkaline phosphatase. These changes were related to postradiation damage, not to recovery.
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PMID:Histochemical and ultrastructural changes in locally gamma-irradiated rabbit intestine. 65 66

This study characterizes the cytochemical properties of the Golgi complex, the structure which corresponds to Golgi complex-endoplasmic reticulum-lysosomes (GERL), and the granule population in luteal cells of guinea pigs at the time of maximum progesterone secretion, in material fixed by vascular perfusion, a method particularly suited for preserving both fine structure and enzyme activity. The distribution of several marker enzymes was determined by electron microscope cytochemistry. Acid phosphatase (ACPase) and arylsulfatase were used to identify structures containing lysosomal proteins. To resolve specific problems, additional cytochemical markers were employed: localization of thiamine pyrophosphatase (TPPase) (in the Golgi complex) and alkaline phosphatase (ALPase) (a plasma membrane marker), and prolonged osmication (a generally accepted method of marking the outer cisterna of the Golgi complex). The results demonstrate that at the time of peak steroid secretion the Golgi complex in luteal cells, in marked contrast to that of most other cell types, typically displays intense ACPase activity in all of its cisternae. Similarly, all Golgi cisternae stain after prolonged osmication and may show TPPase activity. On the other hand, GERL in luteal cells of this age, unlike that in most cells, commonly shows low levels of, or lacks, ACPase activity. However, GERL resembles that of other cell types in being TPPase-negative and in being unstained by treatment with aqueous OsO4. GERL and some Golgi cisternae are reactive for ALPase. The granule population in luteal cells of this stage consists of lysosomes, multivesicular bodies, electrontransparent vacuoles, and microperoxisome-like bodies. These results form a base line with which luteolytic changes described in the companion study (Paavola, L.G. 1978. The corpus luteum of the guinea pig. III. Cytochemical studies on the Golgi complex and GERL during normal postpartum regression of luteal cells, emphasizing the origin of lysosomes and autophagic vacuoles. J. Cell. Biol. 79:59--73.) can be compared.
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PMID:The corpus luteum of the guinea pig. II. Cytochemical studies on the Golgi complex, GERL, and lysosomes in luteal cells during maximal progesterone secretion. 70 77

The postpartum involution of corpora lutea was examined by electron microscope cytochemistry of guinea pig ovaries previously fixed by vascular perfusion, a method which produces optimal preservation of steroid-secreting cells and yet maintains enzyme activity. The intracellular digestive apparatus was identified through the localization of two acid hydrolases, acid phosphatase (ACPase) and arylsulfatase. Other marker enzymes localized were thiamine pyrophosphatase (in Golgi cisternae) and alkaline phosphatase (along plasma membranes). Prolonged osmication was used to mark the outer Golgi cisterna. The results demonstrate that luteal cell regression is characterized by a striking increase in the number of lysosomes and the appearance of numerous, double-walled autophagic vacuoles. Both lysosomes and the space between the double walls of autophagic vacuoles exhibit ACPase and arylsulfatase activity. In contrast to earlier periods, just before and during regression, Golgi complex-endoplasmic reticulum-lysosomes (GERL) is markedly hypertrophied, displaying intense acid hydrolase activity. On the basis of various criteria, GERL is proposed to function in the formation of lysosomes and autophagic vacuoles. Lysosomes seem to develop from GERL as focal protuberances of varying size and shape, which detach from the parent structure. Double-walled autophagic vacuoles, often large and complex in structure, initially are produced as GERL cisternae envelop small areas of cytoplasm. Lytic enzymes, perhaps furnished by the engulfing membranes and trapped lysosomes, presumably bring about digestion of the contents of these vacuoles, producing first aggregate-type inclusions, then, as the contents are further degraded, myelin figure-filled residual bodies. ACPase activity occasionally appears within smooth endoplasmic reticulum tubules and cisternae in advanced regression, possibly suggesting that lytic enzymes utilize this membrane system as an access route to GERL. These data indicate that cellular autophagy is a prominent mechanism underlying luteal cell involution during normal postpartum degeneration of guinea pig corpora lutea. Furthermore they suggest that in regressing luteal cells GERL is responsible for packaging acid hydrolases into lytic bodies.
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PMID:The corpus luteum of the guinea pig. III. Cytochemical studies on the Golgi complex and GERL during normal postpartum regression of luteal cells, emphasizing the origin of lysosomes and autophagic vacuoles. 70 78

The dermal cells in grey, xanthic, and white goldfish integuments were cytochemically characterized for the following enzymatic activities: tyrosinase, DOPA-oxidase, cytochrome oxidase, monoamine oxidase, peroxidase, non-specific esterase, cholinesterase, NAD-diaphorase, NADP-diaphorase, aryl sulfatase, nucleotide phosphodiesterase, beta-glucuronidase, acid phosphatase, alkaline phosphatase, adenosine triphosphatase, thiamine pyrophosphatase, glucose-6-phosphatase, aldolase, as well as succinate, malate, isocitrate, glutamate, glucose-6-phosphate, 6-phosphogluconate, alpha-glycerophosphate, alcohol, lactate, and beta-hydroxybutyrate dehydrogenases. It was found that the epidermis was a significant barrier to the access of cytochemical reaction substrates. Removal of the epidermal barrier provided dermal cell localizations of enzymatic activities which were reproducible. Further, alterations in reaction times and temperatures from the mammalian methodology provided conditions fe various integumental cells were compared for possible interrelationships. The basic foundations for future work with the dermis of poikilothermic vertebrates on an experimental basis were established. In addition, a previously undescribed non-pigmented dermal cell, the "x"-cell, was found to have enzymatic characteristics similar to both melanophores and lipophores. The "x"-cell may be the common precursor of both types of pigment cells.
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PMID:Cytochemical characterization of goldfish (Carassius auratus L.) dermis with special reference to the pigment cells. 82 86

Poly(A)-containing mRNAs labeled with [methyl-3H]methionine were isolated from nucleated erythroid cells obtained from the spleens of anemic mice. The RNAs were further separated into non-globin poly(A)-containing RNAs and highly purified globin mRNA by globin cDNA-cellulose affinity chromatography. DEAE-Sephadex column chromatography of the T2 ribonuclease digestion products of the cDNA-purified globin mRNA fraction yielded methylated resistant fragments with charges of -4.7 (Cap 1) and -5.3 (Cap 2). Digestion of the non-globin RNA fraction revealed a similar pattern with the addition of a methylated mononucleotide identified as 6-methyladenosine at -2 charges. Alkaline phosphatase treatment of the T2 resistant fragments reduced their charges by approximately 2, which is consistent with the removal of one terminal phosphate. Treatment of the globin T2 and alkaline phosphatase-resistant fragments withpenicillium P1 nuclease and alkaline phosphatase yielded a P1-resistant core structure in both fragments. In addition to the core, 2'-O-methylcytidine (Cm) was released from the more negatively charged globin fragment. The P1-resistant cores of the cap structures eluted from DEAE-Sephadex with the known standard m2G5'ppp5'Am and were found to be pyrophosphatase-sensitive establishing a 5'-5'-triphosphate linkage. The pyrophosphatase and alkaline phosphatase digestion products of the globin Cap 1 and Cap 2 core structures were analyzed by high voltage electrophoresis and paper chromatography and found to be 7-methyiguanosine (m7G) and the dimethylated nucleoside 6-methyl-2'-O-methyladenosine (N6mAm). A small amount of the singularly methylated adenosine, 2'-O-methyladenosine (Am) was also observed. The predominant sequences of the methylated nucleosides in the globin cap structures are therefore m7G5'ppp5'N6mAm and m7G5'ppp5'N6mAmpCm.
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PMID:Methylated nucleosides in globin mRNA from mouse nucleated erythroid cells. 83 41


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