Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:BIOD00001 (DNase I)
8,324 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

At various times following estrogen administration, the nuclear matrix was isolated from the liver of male Xenopus laevis by sucrose gradient centrifugation of nuclei treated with a high-salt buffer and DNase I in the presence of a proteolytic inhibitor (PMSC--phenylmethyl sulfonyl chloride). Electron micrographs of the nuclear matrix demonstrate a sponge-like network attached to a well-defined inner envelope with a ribosome-free outer envelope. Chemical analyses show that the HSB-DNase-treated nuclei consist of 16% DNA, 2% RNA, and 82% protein, a composition that is consistent with that of nuclear matrices isolated from other species. The specific activity of the matrix-associated RNA following estrogen treatment appears to be maximally enhanced after 5 h and decreases until approximately 12 h, when the activity begins to increase again.
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PMID:Isolation and characterization of the nuclear matrix from the male Xenopus laevis following estrogen administration: kinetics of [3H] uridine incorporation. 9 25

Viable mutants of polyoma with small deletions ranging in size from 2 to 75 base pairs were obtained by infecting 3T3 cells with polyoma DNA that had been cleaved once with HaeII endonuclease or with DNase-Mn2+ digestion. The HaeII endonuclease-cleaved DNA yielded mutants with deletions at map position 72--73, whereas the mutants generated by DNase I-Mn2+ digestion had deletions either at map position 72--73 or within the map coordinates 92 and 99. Both groups of mutants appeared to grow as well as wild-type virus in 3T3 cells. The deletions at map position 72--73 did not alter the virus's ability to transform rat cells. Hence, the region just to the early side of the origin of DNA replication is not essential for vegetative growth or transformation. But the mutants with deletions in the region between map coordinates 92 and 99, a segment thought to code for polyoma large and middle T antigens (Hutchinson et al., Cell 15:65--77, 1978; Smart and Ito, Cell 15:1427--1437, 1978; Soeda et al., Cell 17:357--370, 1979), transformed rat cells at 0.2 to 0.05 the efficiency of wild-type virus.
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PMID:Construction and analysis of viable deletion mutants of polyoma virus. 22 75

Deoxyribonuclease I has been purified from bovine parotid gland. The purification procedure utilizes an acid extraction of minced parotid gland, salt fractionation, gel filtration, and ion-exchange chromatography. The last step, chromatography on Sulfopropyl-Sephadex, resolves the enzymatic activity into several fractions. The major fraction, designated DNase A, was subjected to further investigation. This enzyme has, as expected, an alkaline pH optimum and an obligate requirement for divalent cations. The presence of calcium chloride protects DNase A from inactivation by proteolytic enzymes. Despite the previously described immunologic dissimilarity, there appears to be a large amount of homology between the parotid and pancreatic DNase's.
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PMID:Purification and partial characterization of deoxyribonuclease I from bovine parotid gland. 26 62

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

Cultured mammary cells from GR mouse were used to analyse proteins associated with the mononucleosomes and released by a short micrococcal DNase treatment of nuclei. On metrizamide density gradients, mononucleosomes appear to be heterogeneous according to their content of associated non-histone proteins. Proteins associated with the denser fraction (1.22 - 1.24 g/ml) were analysed by two dimensional electrophoresis and compared to the proteins released by DNase I treatment. All the proteins associated with mononucleosomes were also released by DNase I treatment. It could then be assumed that these proteins are associated with the active part of the genome. Additional proteins were released by micrococcal DNase treatment of the nuclei. They could be involved in a higher order organization of chromatin.
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PMID:Comparison of non histone proteins selectively associated with nucleosomes with proteins released during limited DNase digestions. 44 Sep 75

Though DNase does not contain any cysteine residues, incubation of the enzyme with 2-nitro-5-thiocyanobenzoic acid in the presence of Ca2+ at pH values above 7.5 results in an irreversible inactivation of the enzyme. The inactivation also occurs when Ca2+ is replaced by Mg2+, but not in their absence. Amino acid analyses after acid hydrolyses of the completely inactivated ant the native enzymes show no significant differences in composition, including tryptophan and half-cystine residues. However, sodium dodecyl sulfate gel electrophoresis indicates enzyme cleavage by the treatment with 2-nitro-5-thiocyanobenzoic acid. This reagent does not inactivate chymotrypsin and lysozyme, and under conditions where bovine DNase is inactivated, does not inactivate other nucleases such as ribonuclease, snake venom phosphodiesterase, and spleen acid DNase. However, it inactivates malt DNase and can, therefore, be considered a specific inhibitor of DNase I. The inactivation kinetics is pseudo-first order, resembling Michaelis-Menten, with an affinity constant of 16.7 mM. It is the cyano group, not the thionitrobenzoic acid of 2-nitro-5-thiocyanobenzoic acid that reacts to form cyano-DNase.
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PMID:Inactivation of bovine pancreatic DNase by 2-nitro-5-thiocyanobenzoic acid. I. A novel inhibitor for DNase I. 48 54

It has been established that nucleosomes are made of histones and DNA fragments. The purpose of this work to establish whether some non-histone proteins are also present in these chromatin subunits. We have found that nucleosome preparations contain phosphorylated non-histone proteins and protein kinases by sucrose gradient analysis. In order to establish whether these proteins are actually bound to nucleosomes or if they represent unbound or aggregated proteins, the following experiments were performed. (a) Free non-histone proteins and proteins released from chromatin by DNase overdigestion were analyzed by sucrose gradient centrifugation. No phosphoproteins but some phosvitin kinase activity was found in the part of the gradient which contained the nucleosomes. It could be assumed that part of the phosphoproteins are bound to nucleosomes. (b) A digestion of nucleosomes with DNase I suppressed the phosvitin kinase activity in the 11-S region of the gradient. (c) High ionic strength, which extracted non-histone proteins, suppressed the phosvitin kinase activity in the nucleosome region. Part of phosvitin kinase and of nuclear phosphoproteins are therefore bound to nucleosomes and are released by nuclease digestion and by high ionic strength.
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PMID:Presence of non-histone proteins in nucleosomes. 68 39

The inhibitory activity in the mitochondrial and postmitochondrial fractions of the liver, spleen and thymus of albino rats was studied with respect to pancreatic DNase I. It is shown to be due to the presence of thermolabile substances of protein nature (natural inhibitors of DNase I) in the subcellular fractions of the organs under study. A higher inhibitory activity is detected in the postmitochondrial fraction of all the tissues under investigation. The lowest inhibitory activity is found in the mitochondrial and postmitochondrial fractions of the liver. The data of a simultaneous study of changes in the activity of tissue DNase and inhibitory activity in the subcellular fractions give reasons to suppose the presence of the nuclease-inhibitory complex in the tissues.
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PMID:[Activity of DNAase I inhibitor in subcellular fractions of rat tissues]. 86 34

Addition of increasing concentrations of autologous DNA, but not of allogeneic DNA, in culture media of human lymphocytes induces a parallel increase of thymidine incorporation into leucocytes and of lymphocytes transformation into blast cells. Specificity of DNA action was analysed by different DNase and RNase treatments. DNase or RNase alone neither stimulates blastic transformation of lymphocytes and incorporation of thymidine into leucocytes, nor inhibits PHA-induced stimulations of these cells. However Dnase--but almost not RNase--clearly inhibits thymidine incorporation and blast transformation induced by autologous DNA.
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PMID:Stimulation of human lymphocytes in vitro by purified autologous DNA. 86 12

1. The filter-paper disc assay for tritium-labeled nucleic acids was modified to reduce washing and manipulation. Evaluation of the procedure indicated greatly enhanced counting efficiency for tritium, complete removal of nuclease digestion products and retention of even nanogram levels of radioactive DNA on the discs in the presence of protein. The modified assay was quite sensitive and had a coefficient of variation of 5.2%. Quite low concentrations of DNase I and endogenous human serum nuclease activity were readily measured by the improved technique, 22 sera yielding a mean value equivalent to about 0.5 ng DNase I/ml serum. We are now using the disc assay to follow serum DNA and DNase levels in patients with autoimmune disorders and various types of cancers.
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PMID:An improved filter-disc assay for 3H-DNA and serum deoxyribonucleases. 91 57


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