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:3.1.21.3 (deoxyribonuclease)
1,528 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Beppu, Michiko (University of Tokyo, Tokyo, Japan), and Kei Arima. Decreased permeability as the mechanism of arsenite resistance in Pseudomonas pseudomallei. J. Bacteriol. 88:151-157. 1964.-The mechanism of arsenite resistance of Pseudomonas pseudomallei strain 54, isolated from soil, was studied by use of radioactive arsenite. Arsenite resistance was found to be related to decreased permeation of arsenite into the cells. P. pseudomallei 54 cells can accumulate arsenite, but the organisms grown adaptively in the presence of arsenite accumulate only a small amount of the drug. Arsenite accumulated in the cells can exchange freely with extracellular arsenite. The apparent dissociation constant of the "bacterium-arsenite complex" was calculated as 5.9 x 10(-5)m for the sensitive cells and 6.3 x 10(-4)m for the resistant ones. No significant difference was observed in the arsenite capacity (maximal uptake) of the cells (2 x 10(-3) mmoles per 30 mg of dry cells). The uptake of arsenite by the sensitive cells was markedly dependent on temperature, but it was not inhibited by 2,4-dinitrophenol (5 x 10(-3)m) and sodium azide (10(-2)m). Omission of the substrate, alpha-ketoglutarate, from the incubation mixture had no inhibitory effect on arsenite uptake. Treatment of the resistant cells with cetyl-trimethylammonium bromide facilitated the uptake of arsenite by the cells. When the sensitive cells accumulating radioactive arsenite were fractionated by the Schmidt-Thanhauser-Schneider method, the large amount of intracellular arsenite was found in the cold perchloric acid-insoluble hot acid-extractable fraction. The arsenite complex with cellular macromolecular constituents cannot be solubilized by treatment with ribonuclease, deoxyribonuclease, and trypsin.
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PMID:DECREASED PERMEABILITY AS THE MECHANISM OF ARSENITE RESISTANCE IN PSEUDOMONAS PSEUDOMALLEI. 1419 80

Hyde, James M. (University of Mississippi School of Medicine, Jackson), Lanelle G. Gafford, and Charles C. Randall. Fine structure of the coat and nucleoid material of fowlpox virus. J. Bacteriol. 89:1557-1569. 1965.-Several morphological forms characteristic of the poxvirus group were demonstrated for fowlpox virus with neutral phosphotungstic acid (PTA). Viral particles (purified from viral inclusion bodies) stained with uranyl acetate (UA) and shadowed with platinum were shown to have an external knobby surface not evident with PTA. The external coat of freshly purified viral particles seemed intact, but as the preparation aged, it appeared to unwind, resulting in twisted "rope-like" structures. This process was facilitated by use of 1% trypsin, and three dense fibrils were identified with UA within the partially detached viral coat. Studies with alkaline PTA (pH 9) were interpreted as revealing a complex nucleoid, but solutions above this pH damaged the particles. The morphology of the nucleoid was better depicted in ultrathin sections of whole virus which, when stained with UA, revealed dense coiled threads. Treatment of virus with sodium lauryl sulfate exposed an underlying coat consisting of small subunits approximately 40 A in diameter. Of great interest was the demonstration that the detergent removed strands of deoxyribonucleic acid (DNA) from the virus without destroying the contour of the particle. The origin of the strands was definitely the fine uranophilic, coiled threads of the nucleoid, which probably represent the DNA molecule(s). That the extracted material was largely DNA was proved by digestion with deoxyribonuclease and resistance to ribonuclease and trypsin. These studies illustrate how a variety of electron microscopic techniques may be utilized alone or in combination to reveal hitherto undescribed fine structure of viral particles.
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PMID:FINE STRUCTURE OF THE COAT AND NUCLEOID MATERIAL OF FOWLPOX VIRUS. 1429 96

Some properties of the cell-free and cell-associated hemolysins of Escherichia coli were studied. Several strains of E. coli that were isolated from intestines of pigs with edema disease produce large quantities of cell-free hemolysin when grown in the presence of an extract of meat. The component of meat that stimulates production of cell-free hemolysin is not extracted by lipid solvents and is not dialyzable. The cell-free hemolysin is an acidic substance that occurs in two forms. It is inactivated by trypsin but not by lecithinase, lysozyme, ribonuclease, or deoxyribonuclease, shows optimum activity between pH 7 and 8, and requires calcium ion for activity. It does not appear to be an enzyme. The kinetics of the lytic reaction are most consistent with the hypothesis that one molecule of cell-free hemolysin is sufficient to lyse one erythrocyte and that it is inactivated in the lytic reaction. The cell-free hemolysin does not sufficiently damage the cell during the prelytic period to cause lysis after the hemolysin-calcium-erythrocyte complex has been disrupted. The cell-associated hemolysin was not separated from the cell by autolysis, freezing, sonic treatment, or treatment with trypsin or lysozyme. It appears to be closely associated with the metabolic status of the cell. Organisms that are highly hemolytic under usual conditions of assay immediately lose most of their hemolytic capability in the presence of sodium cyanide, streptomycin, nalidixic acid, and rifampin.
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PMID:Properties of the Hemolytic Activities of Escherichia coli. 1655 36

Pollack, J. D. (University of Connecticut, Storrs), Shmuel Razin, and Robert C. Cleverdon. Localization of enzymes in Mycoplasma. J. Bacteriol. 90:617-622. 1965.-Cells of eight parasitic and two saprophytic Mycoplasma strains were lysed by use of osmotic shock, and the membranes were separated from the soluble fraction by use of differential centrifugation. Cell fractions were tested for reduced nicotinamide adenine dinucleotide (NADH(2)) oxidase, reduced nicotinamide adenine dinucleotide phosphate (NADPH(2)) oxidase, glucose-6-phosphate dehydrogenase, adenosine triphosphatase, ribonuclease, and deoxyribonuclease activities. Adenosine triphosphatase was confined to the membrane fraction of all Mycoplasma strains. The NADH(2) oxidase activity was associated with the membranes of the saprophytic M. laidlawii and with the soluble fraction of the parasitic Mycoplasma strains. NADPH(2) oxidase activity was detected only in the soluble fraction of the parasitic strains. Glusose-6-phosphate dehydrogenase was demonstrated only in the soluble fraction of M. laidlawii. Ribonuclease activity was found usually in both membrane and soluble fractions, but was generally higher in the membrane fraction. In the human and bovine Mycoplasma strains, deoxyribonuclease activity could not be demonstrated in the soluble fraction; in the remaining strains, activity was highest in the soluble fraction. Dissolution of M. laidlawii strain B membranes by sodium deoxycholate significantly increased membrane-NADH(2) oxidase and adenosine triphosphatase activities.
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PMID:Localization of Enzymes in Mycoplasma. 1656 57

The first method for the direct separation of mesophyll and bundle sheath chloroplasts from whole tissue homogenates of a C(4) plant is described. Centrifugation of mixed chloroplast preparations from Panicum maximum through low viscosity silica sol gradients effectively separates large, starch-containing chloroplasts from smaller plastids. The large chloroplasts are judged to be bundle sheath chloroplasts on the basis of microscopic appearance, the presence of starch grains, the protein complement displayed on sodium dodecyl sulfate acrylamide gels, and the exclusive localization of ribulose bisphosphate carboxylase activity in these plastids. As a measure of intactness both the large (bundle sheath) and small (mesophyll) chloroplasts contain glyceralde-hyde-3-phosphate NADP-dependent dehydrogenase activity that is greatly enhanced by plastid lysis and both chloroplast preparations are impermeable to deoxyribonuclease. Chloroplast enzyme activities are inhibited by silica sol due to the Mg(2+) chelating activity of this reagent. However, well washed chloroplasts separated on silica gradients had enzyme activities similar to reported values in which silica sol gradients were not used.
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PMID:Use of Silica Sol Step Gradients to Prepare Bundle Sheath and Mesophyll Chloroplasts from Panicum maximum. 1666 19

Incubation of barley (Hordeum vulgare L. cv Himalaya) half-seeds with gibberellic acid enhances the secretion of ribonuclease and deoxyribonuclease from aleurone tissue (MJ Chrispeels, JE Varner 1967 Plant Physiol 42: 398-406; L Taiz, JE Starks 1977 Plant Physiol 60: 182-189). These activities were over 50-fold greater in medium of half-seeds incubated with gibberellic acid than in control medium. Ribonuclease and deoxyribonuclease activities initially appeared in the medium 24 to 48 hours after hormone induction and increased for up to 96 hours. Both activities had a pH optimum of 6.0 and a temperature optimum of 55 degrees C. When the medium from gibberellic acid-treated half-seeds was analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis, the major ribonuclease and deoxyribonuclease activity bands comigrated. The two enzyme activities remained associated throughout a 2,700-fold purification employing ammonium sulfate fractionation, Heparin-Agarose affinity chromatography, and Reactive Blue 2-Agarose affinity chromatography. Also accompanying the ribonuclease and deoxyribonuclease activities throughout purification was the ability to hydrolyze the 3'-phosphoester linkage of 3'-AMP. The purified protein was composed of a single polypeptide with an apparent molecular weight of 36 kilodaltons as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. It is concluded that in response to gibberellic acid, barley aleurone tissue secretes a nuclease having ribonuclease, deoxyribonuclease, and 3'-nucleotidase activities.
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PMID:Barley aleurone layers secrete a nuclease in response to gibberellic Acid : purification and partial characterization of the associated ribonuclease, deoxyribonuclease, and 3'-nucleotidase activities. 1666 13

The alterations of deoxyribonuclease DNase activity in cancer cells were the basis of the utilization of mixed vitamins C and K3 in a nontoxic, adjuvant cancer therapy. In order to localize exactly the altered activities of DNase in cancer cells, histochemical methods were utilized. The deficiency of alkaline and acid DNase activity appeared to be characteristic for non-necrotic cells of malignant human and animal tumors. This enzymatic deficiency appeared in experimental carcinogenesis before the phenotypic signs of malignancy. Tumor promoters directly reduced the activity of both DNases. The incidence of spontaneous malignant human and animal tumors appeared to be inversely proportional to the intensity of the activity of both DNases in normal cells and tissues from which these tumors were derived. The fact that alkaline and acid DNase activity was reactivated during the spontaneous and therapeutically induced necrosis of cancer cells suggests that this enzymatic deficiency of DNase activity in cancer cells was due to the action of specific inhibitors of DNases. Characteristic variations of serum alkaline DNase activity in positive responders to therapy, examined in more than 800 cancer-bearing patients, may be the basis for the development of a useful test for therapeutic prognosis and for monitoring of cancer bearing patients. Acid DNase was selectively reactivated in malignant tumor cells by vitamin C (sodium ascorbate), whereas alkaline DNase was reactivated by vitamin K3. Joint vitamin C and K3 administration produced in vitro and in vivo tumor growth inhibition, potentiation and sensitization of chemo- and/or radiotherapy and a decrease in the number of metastases in animals with experimental tumors. Joint vitamin C and K3 administration may be considered as a possible new, non-toxic, adjuvant cancer therapy, which can be easily introduced into the classic protocols of clinical cancer therapy without any supplementary risk for patients.
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PMID:Altered deoxyribonuclease activity in cancer cells and its role in non toxic adjuvant cancer therapy with mixed vitamins C and K3. 1903 2

A new antifungal peptide designated as pomegranin, with an N-terminal sequence resembling that of rice disease resistance NB-S-LRR-like protein, was isolated from fresh pomegranate peels by ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, and gel filtration by fast protein liquid chromatography on Superdex 75. Pomegranin was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel. It exhibited a molecular mass of 11 kDa in both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It inhibited mycelial growth in the fungi Botrytis cinerea and Fusarium oxysporum with an IC(50) of 2 microM and 6.1 microM, respectively. It was devoid of hemagglutinating, ribonuclease, deoxyribonuclease and protease inhibitory activities.
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PMID:Pomegranin, an antifungal peptide from pomegranate peels. 1914 78

Rupture of ACL is a common injury. While the current surgical treatments are effective, many patients still suffer from precocious osteoarthritis, and there is an increasing interest in bioengineering approaches to improve ACL repair. Bovine collagen is a material currently in use for tissue engineering of ligaments. The alpha-gal epitopes found on bovine cells are a source of immunogenic stimulus for human cells. In this study, we wished to determine if those epitopes could be removed sufficiently to mitigate an immunogenic response using either a decellularization protocol or decellularization followed by alpha-galactosidase treatment. Bovine ACLs were treated with Triton-X, sodium deoxycholate, ribonuclease, and deoxyribonuclease to remove cells. A subset of the decellularized tissues was further treated with alpha-galactosidase. Human peripheral blood mononuclear cells (PBMCs) were exposed to untreated, decellularized, and alpha-galactosidase-treated tissues, and PBMC migration and IL-6 release were measured. PBMCs were significantly more attracted to untreated ACL compared to decellularized or alpha-galactosidase-treated tissue, but no difference was seen between the two treatment groups. PBMCs also released significantly more IL-6 when exposed to untreated tissue compared to decellularized ACL or alpha-galactosidase-treated ACL, but no difference was seen between the two treatment groups. Immunohistochemistry using anti-alpha-gal antibody detected the epitopes throughout the untreated ACL, but similar areas of reaction were not seen on decellularized or alpha-galactosidase-treated ACL. These results suggest that our decellularization protocol minimizes the immunogenic reactions of human PBMCs to bovine ACL tissue. Therefore, decellularized bovine ACL tissue may be a safe, effective biomaterial for ACL injury treatments.
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PMID:Decellularization of bovine anterior cruciate ligament tissues minimizes immunogenic reactions to alpha-gal epitopes by human peripheral blood mononuclear cells. 2192 83

In chronic wounds, it may be clinically important to remove extracellular bacterial and patient DNA as its presence may impede wound healing and promote bacterial survival in biofilm, in which extracellular DNA forms part of the biofilm architecture. As medicinal maggots, larvae of Lucilia sericata Meigen (Diptera: Calliphoridae) have been shown to efficiently debride wounds it became of interest to investigate their excretions/secretions (ES) for the presence of a deoxyribonuclease (DNAse) activity. Excretions/secretions products were shown to contain a DNAse, with magnesium, sodium and calcium metal ion dependency, and a native molecular mass following affinity purification of approximately 45 kDa. The affinity purified DNAse degraded genomic bacterial DNA per se, DNA from the slough/eschar of a venous leg ulcer, and extracellular bacterial DNA in biofilms pre-formed from a clinical isolate of Pseudomonas aeruginosa. The latter finding highlights an important attribute of the DNAse, given the frequency of P. aeruginosa infection in non-healing wounds and the fact that P. aeruginosa virulence factors can be toxic to maggots. Maggot DNAse is thus a competent enzyme derived from a rational source, with the potential to assist in clinical wound debridement by removing extracellular DNA from tissue and biofilm, and promoting tissue viability, while liberating proteinaceous slough/eschar for debridement by the suite of proteinases secreted by L. sericata.
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PMID:Blow fly Lucilia sericata nuclease digests DNA associated with wound slough/eschar and with Pseudomonas aeruginosa biofilm. 2282 9


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