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Query: EC:3.1.25.1 (deoxyribonuclease)
 1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A deoxyribonuclease, which requires nucleoside triphosphate for reaction, has been purified about 150-fold from extracts of Bacillus laterosporus. Potassium phosphate and ethylene glycol stabilize the purified enzyme. The enzyme degrades double-stranded DNA about 100 times faster than heat-denatured DNA in the presence of nucleoside triphosphate. Double-stranded DNA is not degraded to any measurable extent in the absence of ATP, but the enzyme exhibits activity toward denatured DNA in the absence of nucleoside triphosphate, and this activity seems to be an intrinsic property of this enzyme protein. The optimum pH is 8.5 and the maximum activity is obtained in the copresence of Mg2+ (8.0 X 10(-3)M) and Mn2+ (7.0 X 10(-5)M). ATP and dATP are most effective and nucleoside di- or monophosphates are ineffective. ATP is converted to ADP and inorganic phosphate during the reaction and the ratio of the amount of ATP cleaved to that of hydrolyzed phosphodiester bonds of DNA is about 3:1. An inhibitor of the enzyme was observed in bacterial extracts prepared by sonic disruption; the inhibitory substance is produced in the bacteria in the later stages of cell growth. Preliminary results show that the inhibitor emerged near the void volume of a Sephadex G-200 column, and was relatively heat-stable, RNase-resistant, and DNase-sensitive.
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PMID:A nucleoside triphosphate-dependent deoxyribonuclease from Bacillus laterosporus. Purification and characterization of the enzyme. 0 Mar 73

Ultrafiltration of protein solutions was investigated, using deoxyribonuclease of Actinomyces streptomycini filtered through a membrane based on vinylpyrrolidone-methyl methacrylate copolymers. It was shown that ionization of the protein molecule, level of the applied pressure as well as the protein concentration in the initial solution influenced particle adsorption on the surface and in pores of the molecule and the formation of gel layer reducing the rate of the solution filtration. The following parameters were found to favor the process: pH=7.5 (the value corresponds to the highest stability of the enzyme and the presence of the total negative discharge on the surface of the protein molecule). DNase concentration not more than 2 mg/ml, pressure 2 atm. The retaining capacity of the membrane was 85% and DNAase losses were 20%.
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PMID:[Effect of several factors on the process of protein solution ultrafiltration]. 1 3

An adenosine triphosphate-stimulated deoxyribonuclease was purified to about 4200 fold from Bacillus cereus. The enzyme activity of the crude extract increased by a factor of about 5 after dialysis. One of the low molecular weight inhibitors of the crude extract was found to be inorganic phosphate. During enzyme purification two nucleases were identified. One of them was specific to denatured DNA and the other one degraded both denatured DNA and native DNA. The activity towards native DNA could be increased several times by ATP. Through all steps of purification the ATP-independent DNase always accompanied the ATP-dependent one and the ratio of their activity was found to be constant. The ATP-dependent DNase also possessed ATPase activity stimulated both by native and denatured DNA. The fact that ATPase was stimulated by DNA and went together with ATP-dependent DNase during purification suggests that these functions belong to the same enzyme complex. Maximal activity of ATPase had broader pH, Mg2+ and ATP concentration ranges than that of DNase. Cooperation of the two functions may be limited only to a narrow range of ATP concentration. Km for ATPase was 1.6x10-4 M ATP.
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PMID:An adenosine triphosphate dependent deoxyribonuclease with adenosine triphosphatase, activity from Bacillus cereus. 4 71

A deoxyribonuclease, called D Nase-1, that is active at acid pH in the presence of EDTA has been studied in Drosophila melanogaster. The locus for the Enzyme maps genetically to 61.8 on the right arm of the third chromosome. Cytogenetically, DNase-1 has been localized to within five to ten bands between 90C-2 and 90E. This analysis utilizes both electrophoretic variants and the Y-autosome translocations of Lindsley et al. (1972). DNase-1 is present in all stages of the life cycle, and the paternal genome actively contributes DNase-1 to the ambryo between 0 and 1 hr after fertilization.
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PMID:A genetic and developmental analysis of an acid deoxyribonuclease in Drosophila melanogaster. 10 79

The action of deoxyribonuclease, ribonuclease, perchloric acid, and pronase on the fine structure of basal bodies of sectioned Paramecium was observed as part of a more extensive autoradiographic electron microscope analysis directed toward the problem of basal body DNA. DNase was found to have no detectable effect on basal body fine structure. Pronase first solubilized the linkers and C tubules of the triplets, then attacked the protein portion of the axosome, a localized portion of the ciliary axoneme adjacent to the distal end of the basal body, the rim fiber, and newly described lumen spiral complex. Prolonged pronase treatment disrupted the remaining microtubular elements, basal body plates, and cartwheel. RNase removed material from the axosome and the lumen complex, a conspicuous structure occupying the central portion of the basal body and consisting of a twisted or looped 90-A diam fiber or, more probably, pair of fibers, in association with large, dense granules. The apparent removal of both RNA and protein from this basal body structure by either of the two corresponding enzymes suggests an unusual organization of the two components. Observations from this and other laboratories suggest that the basal body RNA is single stranded. Its function is unknown but alternatives are discussed.
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PMID:Effects of nuclease and protease digestion on the ultrastructure of Paramecium basal bodies. 17 69

The deoxyribonuclease induced in KB cells by herpes simplex virus (HSV) type 1 and type 2 has been purified. Both enzymes are able to completely degrade single- and double-stranded DNA yielding 5'-monophosphonucleotides as the sole products. A divalent cation, either Mg2+ or Mn2+, is an absolute requirement for catalysis and a reducing agent is necessary for enzyme stability. The maximum rate of reaction is achieved with 5 mM MgCl2 for both HSV-1 and HSV-2 DNase. The optimum concentration for Mn2+ is 0.1 to 0.2 mM and no exonuclease activity is observed when the concentration of Mn2+ is greater than 1 mM. The rate of reaction at the optimal Mg2+ concentration is 3- to 5-fold greater than that at the optimal Mn2+ concentration. In the presence of Mg2+, the enzymes are inhibited upon the addition of Mn2+, Ca2+, and Zn2+. The enzymatic reaction is also inhibited by spermine and spermidine, but not by putrescine. Crude and purified HSV-1 and HSV-2 DNase can degrade both HSV-1 and HSV-2 DNA, but native HSV-1 DNA is hydrolyzed at only 22% of the rate and HSV-2 DNA at only 32% of the rate of Escherichia coli DNA. Although HSV-1 and HSV-2 DNase were similar, minor differences were observed in most other properties such as pH optimum, inhibition by high ionic strength, activation energy, and sedimentation coefficient. However, the enzymes differ immunologically.
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PMID:The deoxyribonuclease induced after infection of KB cells by herpes simplex virus type 1 or type 2. I. Purification and characterization of the enzyme. 20 46

The deoxyribonuclease specified by the recB and recC genes of Escherichia coli (recBC DNase; exonuclease V) has been purified to near homogeneity by a new procedure. Although hydrolysis of even a single nucleotide from a duplex DNA molecule by the pure enzyme is absolutely dependent upon ATP, the extent of phosphodiester hydrolysis is strongly inhibited by ATP concentrations of 0.2 mm or greater, and the initial rate is unaffected. Under these conditions, the extent of DNA hydrolysis is proportional to enzyme concentration. In contrast, neither the rate nor the extent of hydrolysis of single-stranded DNA nor ATP is affected by high concentrations of ATP. The amount of large single-stranded polynucleotide generated by the action of the recBC DNase increases as the ATP concentration increases and, at 0.5 mM ATP, becomes equivalent to the amount of acid-soluble nucleotide formed. These findings suggest that high intracellular concentrations of ATP affect the mechanism of the recBC DNase so as to limit the extent of hydrolysis of duplex DNA, while at the same time favoring the formation of single-stranded regions within the duplex. Such regions may be essential intermediates in the recombination process.
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PMID:On the role of ATP in phosphodiester bond hydrolysis catalyzed by the recBC deoxyribonuclease of Escherichia coli. 31 95

Escherichia coli strains harboring Rtsl were found to excrete extracellular deoxyribonuclease. The DNase activity was greater in cells with pTW2, a mutant from Rtsl.
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PMID:R plasmic Rtsl-mediated production of extracellular deoxyribonuclease in Escherichia coli. 33 89

Specific anti-DNase-I IgG have been used to detect deoxyribonuclease in teratocarcinoma cells by an indirect immunofluorescence method. All the cells studied show fluorescence staining. However, the patterns are quite different in embryonal carcinoma cells (amorphous cytoplasmic fluorescence and absence of nuclear staining) as compared to differentiated cell lines (diffuse, bright granular nuclear and fibrillar cytoplasmic fluorescence). It is possible by this method to distinguish different cell types derived from the same origin. Deoxyribonuclease from teratocarcinoma cells can therefore be considered as a marker of cell differentiation in this system.
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PMID:Immunofluorescence studies on deoxyribonuclease from mouse teratocarcinoma cells during cell differentiation. 39 95

A deoxyribonuclease inhibitor has been purified from KB cells by chromatography on single-stranded DNA-cellulose. Polyacrylamide gel electrophoresis showed the purified preparation to contain two major polypeptides in sodium dodecyl sulfate, with molecular weights of 72,000 and 65,000, but only one major band (with a molecular weight of approximately 140,000) after electrophoresis under nondenaturing conditions. The protein inhibits the hydrolysis of single-stranded DNA by KB DNase, DNase I, DNase II, and nuclease S1, but has no effect on the hydrolysis of double-stranded DNA by these enzymes. The inhibitor causes a reduction in the rate of hydrolysis of DNA by the deoxyribonuclease, probably by reducing the effective concentration of substrate.
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PMID:A deoxyribonucleic acid binding protein from KB cells which inhibits deoxyribonuclease activity on single-stranded DNA. 42 57


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