Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phytase was purified from Aspergillus niger culture fluid by molecular sieve filtration on Sephadex G-200, followed by thermal inactivation of acid phosphatase and CM-cellulose chromatography. The 12-fold purified enzyme had two pH optima at 2.7 and 5.5 and was characterized by high thermal stability in alkaline environment and broad substrate specificity. The Michaelis constant of phytase relative to myo-inositol hexaphosphate sodium salt is 4.8 X 10(-4) M and activation energy 9,217 cal/mole. The molecular weight of the enzyme is estimated at 200,000.
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PMID:Some properties of partially purified phytase from Aspergillus niger. 7 23

The minor enzyme of human prostatic acid phosphatases (pI 5.5) with high specific activity (orthophosphoric monoester phosphohydrolase, acid optimum, EC 3.1.3.2) has been purified for the first time as a pure enzyme protein. The enzyme was a single protein when examined by polyacrylamide gel electrophoresis and isotachophoresis. The specific activity was 1080 micromole per (min X mg) for hydrolysis of 5.5 mmole per liter of p-nitrophenylphosphate at pH 4.8 and 37 C. The purification coefficient was 540 and the recovery of enzyme activity was 2 per cent. The molecular weight of the enzyme subunit when measured by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate was 54,000. The Km of the purified enzyme was 3 X 10(-4) mole per liter for p-nitrophenylphosphate. An antiserum to this enzyme was prepared. The enzyme was cross-reactive with the main enzyme (pI 4.9) of human prostatic acid phosphatases in immunoelectrophoresis. No precipitin arc with the acid phosphatase in the serum of a prostatic carcinoma patient could be shown. Antiserum to the main enzyme caused a precipitin line with the same serum sample.
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PMID:Human prostatic acid phosphatases: purification of a minor enzyme and comparisons of the enzymes. 42 30

A phytase (EC 3.1.3.8) was extracted from rat intestinal bacterium, Klebsiella Sp. No. PG.-2, and purified 50-fold by ammonium sulphate fractionation, ion-exchange chromatography and gel filtration. The enzyme is inducible in nature. The pH optimum was at 6.0 for all the inositol phosphates studied and this characterized the enzyme as an acid phosphohydrolase. Of a range of potential substrates tested, only p-nitrophenyl phosphate alongwith the inositol phosphates was hydrolyzed. It exhibits a Km of 2.0 mM; temperature optimum of 37 degrees C and energy of activation 9,120 cal/mole for all the inositol phosphates studied. The activity was inhibited by Ag2+, Hg2+, Cu2+, fluoride and high substrate concentration.
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PMID:Phytase from Klebsiella Sp. No. PG-2: purification and properties. 216 21

Reaction of the reduced (pink) form of the purple acid phosphatase from beef spleen with excess phosphate at pH 5.0, monitored by optical and low temperature EPR spectroscopy and by measurement of enzymatic activity, results in parallel loss of activity and oxidation of the iron chromophore. Colorimetric and radiochemical (32P) experiments indicate the presence of one mole of tightly bound phosphate in the oxidized (purple) form of the enzyme; this phosphate is released upon reduction. Acid hydrolysis of 32P-phosphate-containing enzyme, followed by high voltage paper electrophoresis, gave no evidence for significant amounts of acid-stable phosphoamino acids.
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PMID:The interaction of phosphate with the purple acid phosphatase from beef spleen: evidence that phosphate binding is accompanied by oxidation of the iron chromophore. 301 Sep 80

At temperatures between 45 and 50 C, staphylococcal acid phosphatase purified 44-fold had maximal activity at pH 5.2 to 5.3. However, the enzyme was most stable in the alkaline range (pH 8.5 to 9.5) at temperatures below 50 C. Iodoacetate and ethylenediamine-tetraacetic acid were effective inhibitors, whereas mercaptoethanol and Cu(2+) acted as stimulators. The energy of activation for hydrolytic cleavage of the synthetic substrate, p-nitrophenyl phosphate, was 19.5 Kcal/mole. K(m) for the same substrate was 4.5 x 10(-4)m. The purified enzyme was most active against the substrates p-nitrophenyl phosphate and glyceraldehyde 3-phosphate.
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PMID:Staphylococcal acid phosphatase: preliminary physical and chemical characterization of the loosely bound enzyme. 497 46

The effect of colchicine on the uptake of oxygen by human leukocytes during phagocytosis of live streptococci or of killed staphylococci was compared with the effect of colchicine on phagocytosis per se, measured in a sensitive bacterial system. The increase in oxygen consumption that normally accompanies phagocytosis was consistently diminished in leukocytes incubated with colchicine in concentrations as low as 2.5 x 10(-6) mole per L (1 mug per ml), and this inhibition was dosage dependent. Yet there was no evidence of decreased phagocytosis with concentrations of colchicine as high as 2.5 x 10(-4) mole per L (100 mug per ml). Furthermore, with measurements at 20, 40, and 60 minutes, the rate of phagocytosis was comparable with and without colchicine.A clue to the dissociation between oxygen consumption and phagocytosis was found in rapidly dried preparations of the incubated leukocytes. Ingested bacteria were present in both control and colchicine-treated granulocytes. In addition, control cells showed normal loss of granules (lysosomal particles) and prominent cytoplasmic vacuoles (digestive vacuoles). Colchicine-treated cells, however, showed less such degranulation and vacuolization. Measurements of granule-associated acid phosphatase activity after phagocytosis support the morphologic observations of less degranulation in colchicine-treated leukocytes. The muted metabolic and morpholgic response to phagocytosis in colchicine-treated cells may be important for the anti-inflammatory effect of colchicine in acute gouty arthritis. Colchicine may also find wider use in defining structure-function dependencies in metabolically stimulated cells.
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PMID:The dissociation by colchicine of phagocytosis from increased oxygen consumption in human leukocytes. 602 83

We have searched for the presence of branching in the chromosomal polymer poly(ADP-ribose) as it occurs in vivo. Treatment of the polymer with phosphodiesterase asnd phosphomonoesterase results in the conversion of internal residues to the nucleoside ribosyladenosine and the conversion of points of branching to diribosyladenosine. We have detected diribosyladenosine in digests of the polymer derived from carcinogen-treated SV40 virus-formed 3T3 cells and in normal rat liver, kidney, and spleen. The frequency of residues involved in branching varied from 0.8 to 1.6 mole % over a 50-fold range of total levels of poly(ADP-ribose). Thus, branching seems to be a general feature of poly(ADP-ribose) as it occurs in vivo.
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PMID:Poly(ADP-ribose) has a branched structure in vivo. 627 56

This study compared the fine structure of macromelanosomes with that of giant melanosome complexes formed through melanosomal autophagocytosis in nevocytes and melanocytes of nevocellular nevi, lentigo simplex and malignant melanoma. While macromelanosomes were found only on rare occasions in these pigmentary disorders [2 of 79 nevocellular nevi (2 junctional nevi), 3 of 12 lentigo simplex and 2 of 93 malignant melanoma], the giant autophagic melanosome complexes were always present, indicating the macromelanosomes are not synthesized simply through melanosomal autophagocytosis. Although both macromelanosomes and giant melanosome complexes exhibited acid phosphatase activity similar to melanosomes, they showed many different ultrastructural features. Characteristically, macromelanosomes contained numerous vesiculoglobular bodies, whereas these bodies were absent in giant melanosome complexes. In those tissues where the presence of macromelanosomes had been ruled out by light microscopy, none of the giant melanosome complexes revealed ultrastructural features indicative of macromelanosomes. Various phases of melanosomal degradation were seen, indicating that they were not simply end-products of lysosomal degradation of melanosomes. It was thought that the key process in the development of macromelanosomes was the accumulation of vesiculoglobular bodies.
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PMID:Comparison of macromelanosomes and autophagic giant melanosome complexes in nevocellular nevi, lentigo simplex and malignant melanoma. 714 20

The sites of dephosphorylating activities histochemically demonstrated in developing limb buds of mammalian and avian species have been reviewed and compared with the pattern of gene expression or of other biochemical properties reported at similar stages in the corresponding sites. Alkaline phosphatase, acid phosphatase, 5' nucleotidase and ATP-phosphohydrolase reactions were studied in mouse, rat and chick embryos. Alkaline phosphatase only was detected in mole limb buds whereas only 5' nucleotidase and ATP-phosphohydrolase were revealed in limb rudiments of macacus rhesus embryos. Five decisive periods or events of limb morphogenesis have been considered successively: (1) the early stages during which the prospective limb constituents acquire limb forming properties and give rise to the young limb buds, (2) the invasion of the limb bud mesoderm by myogenic cells of somitic origin, (3) the ectoderm-mesoderm interactions with particular emphasis on the properties displayed by the apical ectodermal ridge and by the underlying subridge mesoderm of the progress zone, (4) the period of growth and pattern formation along the proximo-distal, anterior-posterior and dorso-ventral axes, with special attention to the properties of the zone of polarizing activity, and (5) the period of tissular predifferentiation particularly as concerns prospective skeletal, musculo-tendinous and connective tissues, with brief comments about growing nerves and blood vessels. At least during the morphogenetic period, most dephosphorylating properties appear independently associated with gene expression or other regional biochemical properties. Many sites of dephosphorylating activity may therefore be considered as interesting markers of ungoing morphogenetic events among which tissue interaction and signalling are frequently concerned.
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PMID:A comparative review of the sites of histoenzymatic dephosphorylating activities and of gene expression in developing limb buds of mammalian and avian species. 926 55

Recombinant phospholipase D (PLD) from Streptomyces chromofuscus (scPLD) has been characterized using colorimetric assays, spectroscopic investigations, and site-directed mutagenesis. scPLD, which shows phosphodiesterase activity toward a wide variety of phospholipids and phosphatase activity toward p-nitrophenyl phosphate, exhibits a visible absorption band with lambda(max) at 570 nm. Metal ion analysis performed by inductively coupled plasma mass spectroscopy shows the presence of approximately 1 equivalent of iron, 0.27 equivalent of manganese, and 0.1 equivalent of zinc per mole of protein as isolated. The metal ion content coupled with the visible absorption feature is compatible with the presence of Fe(3+)-tyrosinate coordination. When scPLD was dialyzed against solutions containing Mn(2+), Zn(2+) or EDTA, the Fe(3+) content was reduced to variable extents, and the residual specific activity correlated well with the residual iron content. Sequence homology with metal ion binding motifs in known alkaline phosphatases and purple acid phosphatase from red kidney bean shows that most of the residues involved in metal ion coordination are conserved among all the sequences considered. Mutation of some of these conserved residues (C123A, D151A, Y154F, and H391A) produced enzymes lacking iron with dramatically reduced PLD activity but little change in secondary structure or ability to bind to small unilamellar vesicles of phosphatidylcholine (with Ba(2+)) or phosphatidic acid. We suggest that scPLD is a member of a family of phosphodiesterase/phosphatases with structural and mechanistic similarity to iron-dependent purple acid phosphatases.
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PMID:An iron-dependent bacterial phospholipase D reminiscent of purple acid phosphatases. 1251 26


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