Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.22.1 (DNase II)
 429 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A macromolecule binding 3H-methylcholanthrene (3H-MCA) and 3H-benzo(a)pyrene (3H-BaP) and sedimenting in the 4-5 S region of sucrose gradient (4.5 S) was identified in rat liver cytosol. The binding was displaced by 100-fold molar excess unlabeled ligands whereas 2,3,7,8-tetrachloro-dibenzo-p-dioxin (TCDD) was ineffective. The dissociation constant for both polycyclic aromatic hydrocarbons (PAHs) was of the order of 10(-8) M or lower. Both 3H-MCA and 3H-BaP bound to 4.5 S in a non covalent manner, since 92% of the bound radioactivity was extractable with ethyl ether. Furthermore the binding was strongly reduced by urea 8 M and by guanidine. HCl 4 M (99 and 70% respectively). Thin layer chromatography of the ethyl ether-solubilized radioactivity showed a peak comigrating with PAHs used as standards. When chromatographed on Sephadex G-200, 4.5 S was eluted as a sharp peak with an apparent molecular weight of 50-60,000 daltons. Enzyme treatment of liver cytosol showed that the 4.5 S binding sites were destroyed by micrococcal nuclease (92% of inhibition). Papain and phosphodiesterase I and II reduced the binding to 50%, whereas DNase I, DNase II, RNase, phospholipase A2 and C and trypsin were ineffective. These data suggest that the PAHs binding macromolecule of rat liver cytosol is a protein associated with a polynucleotide. The binding of both PAHs was enhanced by increasing the incubation temperature, the maximum being reached after 20-30 min at 37 degrees C. After 2.5 min at 65 degrees C, binding sites were completely destroyed. The same temperature-induced "activation" was obtained also by prewarming the cytosol at 37 degrees C in the absence of ligands.
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PMID:Polycyclic aromatic hydrocarbon binding macromolecules. Identification, characterization and temperature activation of a 4.5 S binding nucleoprotein. 406 Feb 44

A fraction of rat-liver chromatin that is transcriptionally active in vivo has been purified 6- to 7-fold over whole chromatin. This was accomplished by selectively shearing chromatin with DNase II followed by fractionating the released portion on the basis of its solubility properties in 2 mM MgCl(2). The resulting soluble material comprises 11% of the total chromatin DNA and is impoverished in histone and enriched in nonhistone protein. Compared with unsheared chromatin, this minor fraction exhibits marked differences in chromosomal protein species. DNA renaturation studies indicate that this fraction is composed of a specific subset of whole genomal DNA sequences. Furthermore, DNA.RNA hybridization experiments suggest that almost 60% of the nonrepetitious DNA sequences of this minor fraction could code for cellular RNA.
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PMID:Partial purification of the template-active fraction of chromatin: a preliminary report. 452 5

Rat liver chromatin has been fractionated into two fractions on the basis of precipitability in standard saline after mild treatment with DNase II. The major portion of liver chromatin contains little nonhistone protein and is enriched in histones, while a minor portion of such chromatin, with which RNA polymerase is associated, is highly enriched in proteins other than histone and impoverished in histones. Although the relative concentrations of the several histone species present in two chromatin fractions are identical, binding of histones to DNA in the minor fractions appears to be modified, presumably by the presence of proteins other than histones.
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PMID:Fractionation of liver chromatin. 528 39

Single oral treatment of rats with acutely toxic doses of diethylnitrosamine (DENA) caused a temporary increase of liver-deoxyribonuclease II (DNase II) in homogenate, parenchymal cell, and diverse cell compartments. Highest stimulation resulted in nuclear fraction and cytosol. Due to largely congruent in vitro features, it was suggested that the normal as well as the DENA-activated DNase II were identical. Non-ionic detergents enhanced the enzyme activity only in control samples to a relatively small extent. Suitable conditions of reaction provided, the activation was suppressed by cycloheximide. The results indicated different mechanisms of DNase II activation in the course of an acute DENA-intoxication: 1. release of structurally bound DNase II fractions into cytosol; 2. induction of the enzyme and/or of an effector; 3. enhancement of the nucleus bound enzyme activity by translocation of activated DNase II from cytosolic to nuclear area.
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PMID:[DNase II activation in rat liver in the course of acute diethylnitrosamine-induced damage (author's transl)]. 617 Feb 74

The histone content of zinc-deficient (-Zn) Euglena gracilis decreases while, concomitantly, DNA content increases and the transcription rate is reduced markedly [Mazus, B., Falchuk, K. H., & Vallee, B. L. (1983) Biochemistry (in press); Falchuk, K. H., Fawcett, D. W., & Vallee, B. L. (1975) J. Cell Sci. 17, 57-78]. The effects on major constituents of the genome have been examined by studying the rate and extent of hydrolysis of +Zn and -Zn chromatin by micrococcal nuclease, DNase I, or DNase II. The size of hydrolyzed DNA fragments suggests similarity of the +Zn E. gracilis chromatin organization to that of other eukaryotes. The major protein constituent of -Zn chromatin is a polypeptide of less than 3000 daltons whose electrophoretic mobility differs from that of any known histone components of chromatin, the latter described elsewhere (K. H. Falchuk et al., unpublished results). This protein profoundly affects the structure of -Zn chromatin, which is about 10-30-fold more resistant to micrococcal nuclease hydrolysis than +Zn chromatin. Moreover, the resultant DNA fragments [2000 base pairs (bp)], are much larger than those of +Zn cells. Under conditions which hydrolyze +Zn chromatin into DNA fragments smaller than 50 bp, only 50% of -Zn chromatin is digested into fragments less than 2000 bp, i.e., in the range of those expected for oligonucleosomes. Removal of the low molecular weight protein from -Zn chromatin reverses its enhanced resistance to nucleolysis and results in extensive hydrolysis. Conversely, addition of the low molecular weight protein to +Zn chromatin increases the resistance of this complex to digestion.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Composition and structure of zinc-deficient Euglena gracilis chromatin. 622 50

Extracts of bull and ram sperm tails were prepared by DTT and CTAB treatment. Such extracts contained deoxyribonuclease II, degrading only native double-stranded DNA at acid pH (3.9--4.5). At least three distinguishable DNase II activities were found in these extracts as judged by their sensitivity to thiol compounds and various anions and cations. The deoxyribonuclease II activity is apparently located in or in association with the mitochondria.
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PMID:DNase II in bull and ram sperm tail and mitochondria. 624 97

The acid deoxyribonucleases [DNase II; EC 3.1.4.6] in human urine were purified approximately 400- to 500-fold by phosphocellulose chromatography, gel filtration on Sephadex G-75 and isoelectric focusing, with a total recovery of 22%. The enzymes were present in a least three forms with different isoelectric points, pHs 6.4, 6.6, and 6.8. However, other properties were essentially similar. The enzymes did not require divalent cations for activity, and the optimal pHs were at 5.1 to 5.3 in 33 mM acetate buffer. They had a molecular weight of around 36,000, as estimated by gel filtration on Sephadex G-75. The enzymes were endonucleases which hydrolyzed native, double-stranded DNA about 5 to 15 times faster than thermally denatured DNA. The products formed from native DNA were 3'-phosphoryl- and 5'-hydroxy-terminated oligonucleotides. The average chain length of the limit digests with these enzymes was approximately 11 to 15, and the major fragments were longer than pentanucleotides. The final preparations were free of nonspecific acid and alkaline phosphatases and phosphodiesterase, but contained contaminating ribonuclease activity.
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PMID:Purification and properties of deoxyribonuclease II from human urine. 624 3

Musoca from bovine small intestine was homogenized in Krebs-Ringer phosphate buffer, pH 7.8 the homogenate centrifuged at 16300 X g, and the supernatant solution filtered through cheesecloth to remove lipid material. The filtrate was centrifuged at 105000 X g and the supernatant solution chromatographed on DEAE-cellulose. The major peak of DNase II activity, eluted with 20 mM phosphate - 10 mM EDTA buffer, pH 7.8, was purified further by ion-exchange chromatography on CM-cellulose and gel filtration on Sephadex G-100. The enzyme was purified 78-fold in 13% yield. Evidence was adduced to indicate that the second minor peak of DNase II activity, eluted from the DEAE-cellulose by a potassium chloride gradient in the 20 mM phosphate - 10 mM EDTA buffer, was an artifact arising from the presence of significant amounts of DNA in the 105000 X g supernatant. The enzyme degraded DNA endonucleolytically to 3'-PO4, 5'-OH oligonucleotides and is similar in its properties to DNase II from other tissues.
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PMID:Isolation of deoxyribonuclease II from bovine intestinal mucosa. 625 55

The precise locations and relative exposures of the DNase II-accessible sites in the nucleosome core DNA are determined using techniques previously employed for the enzyme DNase I. It is found that there are a number of similarities between the site exposure patterns for the two enzymes but that in general the DNase II seems to discriminate less among adjacent sites' accessibilities than does DNase I. The two enzymes attack essentially the same positions in the DNA, the average difference between the precise location of the site being less than one-half base for the two enzymes. Such close similarities in the digestion patterns of two enzymes with such different mechanisms of scission show that the patterns reflect the structure of the nucleosome core and not merely the properties of the particular enzyme used.
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PMID:DNase II digestion of the nucleosome core: precise locations and relative exposures of sites. 627 1

Chromatin fragments released from intact Friend erythroleukemia cell nuclei during limited incubation with micrococcal nuclease, DNase II or DNase I were analyzed to determine the distribution of DNA methyltransferase in chromatin. The enzyme was released in a free form when internucleosomal DNA was digested with micrococcal nuclease but was found associated with Mg++-precipitable polynucleosomes after DNase II digestion. Less than 25% of the enzyme was released from nuclei incubated with DNase I under conditions where transcriptionally active chromatin should have been completely digested. These results indicated that the bulk of DNA methyltransferase was bound to "linker" DNA in condensed regions of chromatin. Preferential rebinding of free enzyme to linker DNA was also demonstrated in vitro. The possibility that chromatin proteins play a role in regulating access of DNA methyltransferase to specific sites in DNA is discussed in light of these findings.
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PMID:Localization of DNA methyltransferase in the chromatin of Friend erythroleukemia cells. 627 20


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