Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.25.1 (deoxyribonuclease)
 1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Data on the role of oral lysozyme, ribonuclease, deoxyribonuclease and peroxidase in antimicrobial defense of the macroorganism are reviewed. The biochemical and physiological properties of the enzymes secreted by salivary glands and released from emigrating leukocytes are discussed. Spectra of antimicrobial action of the enzymes and participation of these enzymes in maintaining the stability of oral biocenosis are described as well as the regulation of these enzymatic activities and the pathogenetic significance of impairments in their secretion. The most perspective aspects of the problems discussed are outlined for further investigation.
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PMID:[Enzymatic mechanisms for antimicrobial protection of the oral cavity]. 20 88

A pancreas-specific antigen was identified by immunologic techniques and purified from saline extract of human pancreas. The purified pancreas-specific antigen was shown to be homogeneous by polyacrylamide gel electrophoresis under both denaturing and non-denaturing conditions. It had a molecular weight of 44000 as estimated by gel filtration or sodium dodecyl sulfate-gel electrophoresis, and a sedimentation coefficient of 3.4 S as analyzed by sucrose gradient centrifugation. Pancreas-specific antigen possessed an isoelectric point of 4.9 and migrated to alpha-beta region upon immunoelectrophoresis. By colorimetric assay procedures, pancreas-specific antigen exhibited no enzyme activity, such as amylase, protease, esterase, lipase, acid phosphatase, alkaline phosphatase peroxidase, deoxyribonuclease or ribonuclease. Immunoreactivity of pancreas-specific antigen was sensitive to proteolytic enzymes, perchloric acid and high temperature (70 degrees C, 10 min); but insensitive to neuraminidase or beta-glucosidase. Immunohistochemical staining revealed that pancreas-specific antigen was located in acinar cells of human pancreas. In addition, a higher concentration of pancreas-specific antigen was detected in pancreatic juice than in the saline extract of pancreas. This newly identified pancreas-specific antigen, therefore, may be a useful marker protein in physiological studies of pancreas and pancreatic secretion.
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PMID:Purification and characterization of a human pancreas-specific antigen. 678 69

Low dosages of chloramphenicol (25-50 micrograms/ml) brought about a 2-4-fold stimulation of acid phosphatase activity in 48 h-germinated cotton (Gossypium hirsutum) embryos. However, at high concentrations of chloramphenicol (100-1000 micrograms/ml), there was a progressive decline in enzyme activity. The stimulatory effect of the drug on acid phosphatase activity was relatively specific, since no significant stimulation of activities of proteinase, deoxyribonuclease, ribonuclease, o-diphenolase and peroxidase was observed in germinating cotton embryos. Chloramphenicol, however, did promote the activities of isocitric lyase and alkaline phosphatase. Sephadex G-200 chromatography of the enzyme fraction revealed high (230 000)- and low (106 000)-molecular-weight multiple forms of acid phosphatase in the chloramphenicol-treated embryos, in contrast with a single molecular form (mol.wt. 106 000) in the untreated embryos. Thus the treatment of cotton embryos with chloramphenicol induced both a qualitative and a quantitative change in the acid phosphatase activity. Chloramphenicol-stimulated acid phosphatase activity was strongly inhibited when Pi was included in the germination medium. However, the control embryos showed less pronounced inhibition of enzyme activity in presence of Pi ions.
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PMID:Chloramphenicol stimulates acid phosphatase activity in germinating cotton (Gossypium hirsutum) embryos. 687 Aug 57

Early detection of testicular leukaemia and the identification of residual leukaemic cells in treated patients are important aims in the management of males with acute lymphoblastic leukaemia (ALL). In most cases of ALL ( greater than 95%) the blast cells express terminal deoxynucleotidyl transferase (TdT), a nuclear enzyme. We have therefore standardized the immuno-fluorescence and -peroxidase techniques (using anti-Tdt antibodies) for identifying TdT cells in the normal thymus, as well as in samples of testis with heavy leukaemic infiltrates (positive controls). TdT cells can be identified in formalin (but not in Bouin's or Carnoy's) fixed paraffin-embedded tissues, and the preservation of morphological details is excellent. The method is nevertheless difficult to standardize and also requires the use of deoxyribonuclease (DNase) for the digestion of sections. However, in frozen tissue sections, stronger staining of TdT cells was found, even without DNase treatment. Good morphology was preserved when cut sections were fixed immediately in the cryostat. In the second part of the study 15 samples from treated boys were analysed to see whether the technique is suitable to identify residual minimal leukaemic infiltrates. In 5 patients scanty disseminated TdT cells were detected, and in 2 patients small clumps of TdT cells were seen. The results indicate that the immunohistological identification of TdT ALL blasts may be the method of choice.
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PMID:Nuclear terminal deoxynucleotidyl transferase in leukaemic infiltrates of testicular tissue. 704 2

The mechanism of Cd2+ on the DNA cleavage and Ce3+ on the DNA repair in the kidney of silver crucian carp (Carassius auratus gibelio) is investigated by agarose gel electrophoresis methods and assaying biochemical indexes. It proves that Cd2+ induces the classical laddering degradation of DNA in vivo, but DNA cleavage is repaired after injecting with a low Ce3+ concentration under various Cd2+ concentrations. The DNA cleavage caused by Cd2+ is the result of the activation of deoxyribonuclease (DNase) and accumulation of reactive oxygen species (ROS), and Cd2+ destroys the antioxidant system, which diminishes the activities of superoxide dismutase, catalase, and peroxidase, and the increase of the lipid peroxidation (LPO) level. However, Ce3+ could inhibit activation of Cd2+ on DNase activity, relieve inhibition of Cd2+ on activities of the antioxidant enzyme, and diminish ROS accumulation. The results show that Ce3+ could relieve the toxicity of Cd2+ to silver crucian carp.
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PMID:Regulative mechanism of Ce3+ relieves DNA damage caused by Cd2+ in the kidney of silver crucian carp. 1719 24

The subject of acute injury, apoptosis and canceration of animals induced by heavy metal ions has been one of the hotspots studied worldwide. However, the exact molecular mechanism of Cd-induced carcinogenicity remains largely unclear, and how to relieve the toxicity in vivo has rarely been reported. For this paper, we have investigated the mechanism of Cd2+ on DNA cleavage and Ca2+ on DNA repair in the liver of silver crucian carp (Carassius auratus gibelio) by agarose gel electrophoresis methods and by estimating biochemical indexes. Our results show that Cd2+ induces the classical laddering degradation of DNA in vivo and that DNA cleavage is repaired after injection with Ca2+ under various Cd2+ concentrations. DNA cleavage caused by Cd2+ is due to the activation of deoxyribonuclease (DNase) and the accumulation of reactive oxygen species (ROS). Furthermore, Cd2+ destroys the antioxidant system, which diminishes the activities of superoxide dismutase (SOD), catalase (CAT) and peroxidase (POD), causing an increase of the lipid peroxidation (LPO) level, respectively. However, after the liver is injected with Ca2+ under various Cd2+ concentrations, the DNase activity, the ROS generating rate and the LPO level are obviously reduced, the activities of SOD, CAT, and POD are greatly increased. At the same time, ROS production and removal recoves its balance. The results show that Ca2+ can relieve the toxicity of Cd2+ in silver crucian carp.
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PMID:Mechanism of Cd2+ on DNA cleavage and Ca2+ on DNA repair in liver of silver crucian carp. 1864 22

A highly sensitive and ultrasensitive electrochemical aptasensor for platelet-derived growth factor BB (PDGF-BB) detection is fabricated based on layered molybdenum selenide-graphene (MoSe2-Gr) composites and Exonuclease III (Exo III)-aided signal amplification. MoSe2-Gr is prepared by a simple hydrothermal method and used as a promising sensing platform. Exo III has a specifical exo-deoxyribonuclease activity for duplex DNAs in the direction from 3' to 5' terminus, however its activity is limited on the duplex DNAs with more than 4 mismatched terminal bases at 3' ends. Herein, aptamer and complementary DNA (cDNA) sequences are designed with four thymine bases on 3' ends. In the presence of target protein, the aptamer associates with it and facilitates the formation of duplex DNA between cDNA and signal DNA. The duplex DNA then is digested by Exo III and releases cDNA, which hybridizes with signal DNA to perform a new cleavage process. Nevertheless, in the absence of target protein, the aptamer hybridizes with cDNA will inhibit the Exo III-assisted nucleotides cleavage. The signal DNA then hybridizes with capture DNA on the electrode. Subsequently, horse radish peroxidase is fixed on electrode by avidin-biotin reaction and then catalyzes hydrogen peroxide and hydroquinone to produce electrochemical response. Therefore, a bridge can be established between the concentration of target protein and the degree of the attenuation of the obtained signal, providing a quantitative measure of target protein with a broad detection range of 0.0001-1 nM and a detection limit of 20 fM.
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PMID:Ultrasensitive sensing platform for platelet-derived growth factor BB detection based on layered molybdenum selenide-graphene composites and Exonuclease III assisted signal amplification. 2638 5

Notorious bacterial biofilms are becoming severe threats to public health worldwide. As the important component in biofilm extracellular polymeric substances (EPS), extracellular DNA (eDNA) has been manifested to connect different EPS components and bacteria together, leading biofilms hard to eliminate. Herein a series of MOF/Ce-based nanozymes with deoxyribonuclease (DNase) and peroxidase mimetic activities have been designed and synthesized for combating biofilms. The cerium (IV) complexes (DNase mimics) are capable of hydrolyzing eDNA and disrupting established biofilms, while the MOF with peroxidase-like activity can kill bacteria exposed in dispersed biofilms in the presence of H2O2. This can avoid the recolonization of bacteria and recurrence of biofilms. Given the fact that single-modal antibacterial agent is difficult to drastically eradicate biofilms, the marriage of two kinds of nanozymes is a rational strategy to acquire enhanced performance in combating biofilms. Besides, the utilization of nanozymes circumvents drawbacks of natural enzymes which are costly and vulnerable. Further studies have demonstrated that this kind of artificial enzyme with dual enzyme-mimetic activities can penetrate the biofilms, and inhibit bacterial biofilm formation intensively. Consistently, in vivo anti-biofilm application in treating subcutaneous abscess exhibits commendable wound healing and admirable bactericidal effect. To the best of our knowledge, it is the first time to devise an integrated nanozyme based on the peroxidase-like activity of MOF to eliminate biofilms and kill bacteria on site. This work may promote the application of MOF in the antibacterial field.
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PMID:A series of MOF/Ce-based nanozymes with dual enzyme-like activity disrupting biofilms and hindering recolonization of bacteria. 3098 10