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 existence of a specific inorganic pyrophosphatase (PPi ase), distinct from alkaline phosphatase in bone has been suggested but is often regarded as questionable. In the present investigation, several features of PPi ase activity have been demonstrated, which suggest that it represents an enzyme protein different from those splitting phosphomonoesters and ATP. PPi ase was largely destroyed during extraction with n-butanol, which facilitated the solubilization of alkaline phosphatase and ATP splitting enzymes and only partially destroyed acid phosphatase. Two major groups of phosphate esters and pyrophosphates splitting enzymes were separated by gel filtration from homogenates of rat bones. The first pool contained high ATP-ase and phosphomonoesterase activities, but only low activity against inorganic pyrophosphate (PPi) in the presence of MgCl2. The second pool was most active against PPi at pH 7.5 in the presence of excess MgCl2 and only slightly hydrolyzed phosphomonoesters or ATP. Immunodiffusion showed that these 2 pools contained 2 distinct proteins. It was concluded that there exists a specific inorganic pyrophosphatase distinct from phosphomonoesterases and ATP-ases in bone tissue.
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PMID:Inorganic pyrophosphatase activity distinct from alkaline phosphatase in rat bone. 59 70

Fragments of rat liver mitochondrial DNA were isolated. In vivo these fragments were able to form the complexes with the proteins of inner mitochondrial membrane. The fragments represent unique DNA regions with the secondary structure, their A-T content being equal to 82%. With the aid of phosphomonoesterase, polynucleotidkinase and gamma-(32P)-ATP mtDNA fragments were labeled and analyzed for oligopyrimidine composition. It was shown that they were enriched in di- and tri-oligo-pyrimidine blocks. The fragments are shown to form in vitro a complex with the membrane proteins. A single protein m. wt. 40,000) was reisolated from the complex.
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PMID:[Isolation and characteristics of DNA fragments bound to mitochondrial membrane proteins]. 61 37

Biotin administration to old rats (28 months) causes in the blood an increase of ATP, glucose, triglycerides, alkaline phosphatase and a decrease of cholesterol and acid phosphatase; in the liver DNA and electrostatic interactions between DNA and histones are increased. Such parameters come within the values shown by adult rats.
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PMID:Biotin as a regulator of some haematic parameters and of DNA-content of the liver of old rats. 62 48

Liver function tests were performed in severe and mild diabetic rats and under the influence of ATP. In mild diabetics the serum cholesterol was significantly increased, while in severe diabetes the serum cholesterol was significantly lower than in mild diabetes. The decreased serum cholesterol in severe diabetes may be an indication for the development of fatty liver. The serum alkaline phosphatase and serum bilirubin were significantly increased in both the severe and mild diabetic states, while the thymol turbidity test was insignificantly changed in both states of diabetes. Serum albumin was significantly decreased in 10 days mild diabetes, while it was insignificantly changed in 48 hrs severe diabetic animals. The effect of ATP was investigated in mild diabetes. ATP resulted in a significant increase in serum albumin and a decrease in total globulins with the resultant increase in A/G ratio. The serum alkaline phosphatase exhibited a significant reduction under the influence of ATP. The elevated cholesterol of mild diabetic rats remained significantly elevated and was not reduced by ATP, though the fat content of the liver showed a significant reduction. This may be due to more rapid mobilisation of fat from the liver under the influence of ATP. ATP showed no significant effect on serum bilirubin and thymol turbidity test. the histopathological examination of the liver revealed that administration of ATP to alloxan diabetic rats had a beneficial effect. It resulted in disappearrance of the fat globules from the liver cells.
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PMID:Effect of ATP on liver function tests in experimental diabetes. 65 50

The location of the protein bound to bacteriophage phi29 DNA has been studied with restriction endonucleases, exonucleases, and polynucleotide kinase. The protein is invariably associated with the two terminal DNA fragments generated by restriction endonucleases. The phi29 DNA prepared with or without proteinase K treatment is resistant to the action of the 5'-terminal-specific exonucleases, lambda-exonuclease and T7 exonuclease. The phi29 DNA is also inaccessible to phosphorylation by polynucleotide kinase even after treatment with alkaline phosphatase. On the other hand, phi29 DNA is sensitive to exonuclease III, and the 3' termini of the DNA can be labeled by incubating with alpha-[32P]ATP and terminal deoxynucleotidyl transferase. The protein remains associated with the phi29 DNA after treatment with various chaotropic agents, including 8 M urea, 6 M guanidine-hydrochloride, 4 M sodium perchlorate, 2 M sodium thiocyanate, and 2 M LiCl. These results are consistent with the notion that the protein is linked covalently to the 5' termini of the phi29 DNA.
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PMID:Bacteriophage phi29 terminal protein: its association with the 5' termini of the phi29 genome. 73 97

Using a quantitative cytochemical method, explanted calvaria of 1- to 6-day-old male rats were used for the measurement of the in situ effect of parathyroid hormone (PTH) on the activity of alkaline phosphatase (AP) in the calcifying bone. The earliest effect of PTH was observed at 4--7 min. The direction and magnitude of the response of AP was dependent on the age of the animal and on the dose of PTH (50 fg-500 pg/ml). The calvaria of younger animals (2-days old) showed a decrease in AP activity, whereas in 5-day-old rats, AP activity was stimulated by PTH. In 5-day-old animals, the linear dependence of ATP stimulation on the PTH dose in the concentration range 50 fg-50 pg/ml could serve as the basis for a bioassay of a high sensitivity. The age-dependent response of AP to PTH may reflect the difference between the early and late stages of the calcification process. Our observations may reconcile conflicting reports on the effect of PTH on bone AP.
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PMID:Early effects of parathyroid hormone on rat calvarian bone alkaline phosphatase. 74 3

Using histochemical techniques, changes in the localization of different reserve substances (e.g. pectic compounds, starch, polysaccharides, proteins, nucleic acids, ascorbic acid) and enzymes (Acid phosphatase, alkaline phosphatase, ATP-ase, 5-nucleotidase, esterase, phosphorylase, succinate dehydrogenase, cytochrome oxidase and lipase) have been studied in the young and fertilized ovules of Zephyranthes sp. and Lagenaria sp. etc. Extensive changes in the enzyme activity and reserve substances are demonstrated during megasporogenesis and megagametogenesis and most of the substances exhibited interesting distributional pattern. Similarly, all the enzymes investigated have specific locale of distribution in the tissues which displayed differentiation of embryo sac. The earlier changes observed are in the megaspore which contained many reserve substances (starch; nucleic acids; ascorbic acid; proteins) and enzymes (peroxidase, succinate dehydrogenase, acid phosphatase, alkaline phosphatase and ATP-ase). In the matured embryo sac different cells have differential localization of the substances. Based on histochemical studies, distinct differences are made out between egg and synergids; egg and central cell. In general antipodals have maximum accumulation of physiologically active substances and intense activity of different enzymes. Nucellus cells also stored diverse substances and enzymes especially towards the chalazal end. Pollination stimulated accumulation of several reserve substances and enzymes in the tip of nucellus beak, micropylar zone and these included starch, peroxidase, phosphorylase succinate dehydrogenase, cytochrome oxidase etc.
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PMID:Physiology of sexual reproduction. I. A histochemical study of the embryo sac development in Zephyranthes rosea and Lagenaria vulgaris. 81 Oct 56

32P-labeled cowpea mosaic virus (CPMV) RNAs were analyzed for their 5' termini by three different fingerprinting standard procedures. These analyses showed unequivocally that CPMV RNAs lack a structure like m7GpppN ... at their 5' termini. In addition, neither mono-, di- or triphosphorylated [(p)(p)pN ....] termini were found in the respective fingerprints. The inability to label the 5' termini treatment with gamma-32P-ATP and polynucleotide kinase, either per se or after pretreatment with alkaline phosphatase, strongly suggests the absence of a free 5'-OH and a free 5'-phosphate at the 5' terminal nucleotide in CPMV RNAs. The various analyses also showed that no 2' -O-methylated nucleotides, N6-methyladenosines or pseudo-uridines are present in CPMV RNAs.
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PMID:Cowpea mosaic virus RNAs have neither m7GpppN ... nor mono-, di- or triphosphates at their 5' ends. 87 20

The 5'-phosphomonoesterase activity of 5'-nucleotidase (EC 3.1.3.5) and alkaline phosphatase (EC 3.1.3.5) participates in the catabolism of purine ribonucleotides to uric acid in humans. Initial velocity studies of 5'-nucleotidase suggest a sequential mechanism of interaction between AMP nad MgCl2, with a Km of 14 and 3 muM, respectively. With product inhibition studies the apparent Ki's for adenosine, inosine, cytidine, and inorganic phosphate were 0.4, 3.0, 5.0, and 42 mM, respectively. A large number of nucleoside mono-, di-, and tri-phosphate compounds were inhibitors of the enzyme. Allopurinol ribonucleotide, ADP, or ATP were competitive inhititors when AMP was the substrate, with a Ki slope of 120 muM. The phosphomonoesterase activity of human placental microsomal alkaline phosphatase had a pH optimum of 10.0 and had only 18% of maximum activity at pH 7.4. Substrates and inhibitors included almost any phosphorylated compound. The Km for AMP was 0.4 mM and the apparent Ki for Pi was 0.6 mM. Activity was increased only 19% by 5 mM MgCl2. These observations suggest that 5'-nucleotidase and alkaline phosphatase may be inhibited by ATP and Pi, respectively, under normal intracellular conditions, and that AMP may be preferentially hydrolyzed by 5'-nucleotidase.
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PMID:Purine catabolism in man: inhibition of 5'-phosphomonesterase activities from placental microsomes. 101 16

Rats kept on a low-magnesium diet for 14 weeks developed increasing clinical symptoms, from slight trophic changes to inhibition of growth. Focal fragmentation of myocardial fibers was followed by focal fuchsinophilia and later--by focal necrosis. Increasing morphological lesions were associated with calcium salts deposition in the degenerated myocardial fibers, connective tissue and wall of cardiac blood vessels. The low-magnesium diet did not affect the activity of ATP-ases and cytochrome oxidase. The areas of myocardial degeneration and necrosis were free of the activity of alkaline phosphatase and succinic dehydrogenase.
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PMID:Effect of low-magnesium diet on the histology and the activity of certain enzymes of rat myocardium. 122 2


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