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

The deoxyribonuclease activities from human lymphocytes have been compared with the activities from acute lymphocytic leukemic cells and mouse leukemic cells L5178Y using the in situ detection of deoxyribonucleases in DNA-containing polyacrylamide gels following their separation by micro-disc-electrophoresis. A neutral deoxyribonuclease activity is completely missing in leukemic cells of untreated patients while a group of acid deoxyribonuclease activities is increased. A similar deoxyribonuclease pattern can be seen in L5178Y cells. Under medical treatment the increment of the acid deoxyribonuclease activities disappears and the neutral deoxyribonuclease activity reappears.
 ...
PMID:Deoxyribonucleases activities in human leukemic cells and mouse lymphoblasts. 107 Oct 14

Rabbit antibovine spleen DNase II and antihuman parotid amylase IgG were coupled to zirconium-clad (MAO, Corning) or plain (GAO, Corning) glass beads. (These were challenged with DNase II or amylase (human parotid or pancreatic), respectively. Although columns of the beads bound the enzymes whereas control columns did not, recoveries from the immune adsorbents were not only not quantitative but extremely variable. The columns also shed material absorbing in the ultraviolet. The antiamylase IgG-MAO column bound amylase so firmly, yet without inactivating it, that an insoluble enzyme reactor was formed. For these experiments, amylase was labeled with 14C in vitro without loss of activity.
 ...
PMID:Studies on the reproducibility of glass bead antibody affinity columns. 108 Jan 56

Collagenase perfusion of the liver followed by pronase treatment of the cell suspension thus obtained gave a quantitative recovery of viable nonparenchymal liver cells (NPC). From these NPC, Kupffer (K) cells can be purified by attachment to tissue culture dishes. Tail vein injection of carbon 1-2 h before liver perfusion permitted stepwise calculation as well as visualization of carbon-containing K cells. When these K cells have been put into tissue culture medium with serum and incubated overnight, they exhibit typical macrophage characteristics. Phase-contrast and transmission electron microscopy showed typical macrophage morphology and scanning electron microscopy revealed well-spread cells with cytoplasmic projections and ruffled membranes. Endocytosis studies using radioactive colloidal gold and inert latex particles also indicated that these cells are highly active in pinocytosis and phagocytosis. Further characterization of K cells is the identification of Fc receptor on their membranes. Studies on lysosomal enzymes showed that purified K cells possess higher specific activities in beta-glucuronidase, acid DNase, and cathepsin D than in purified parenchymal cells.
 ...
PMID:Mass isolation and culture of rat kupffer cells. 109 Jun 96

A special class of non-histone protein ("tight protein") is identified in purified HeLa cell chromatin on the basis of its failure to dissociate from the DNA at very high ionic strength (2.5 M NaCl-5.0 M urea), where over 92% of the total chromatin protein is released. The tight proteins are insoluble in 0.4 N H2SO4 and lack histones as determined by polyacrylamide gel electrophoresis. They have molecular weights between 14,000 and 85,000 with over 70% of the polypeptide chains between 14,000 and 30,000 mol wt. This is the same size range as the non-histone proteins which others have found to display species-specific DNA binding in vitro. There is approximately one molecule of tight protein per 275 DNA base pairs. The tight proteins are characterized by much higher rates of labeling with amino acids than the histones and non-histone chromatin proteins that are dissociated from the DNA by high ionic strength, but they have the lowest phosphorylation levels. Chromatin fractionation experiments were performed to investigate the distribution of tight proteins between template-active and template-inactive regions. Under specific conditions, spleen DNase (DNase II) selectively shears those portions of HeLa cell chromatin that contain nascent RNA transcripts. This nascent RNA-enriched chromatin fraction also contains a high level of the proteins known to be complexed with heterogeneous nuclear RNA in ribonucleoprotein particles and contains over 70% of the RNA polymerase activity of total chromatin. When this method was employed to investigate the distribution of tight proteins, they were found to be almost entirely confined to the template-inactive fraction. Although these experiments do not elucidate the precise function of these proteins, they identify, for the first time, a particular subclass of non-histone chromosomal protein which is distributed asymmetrically between transcriptionally active and inactive chromatin regions.
 ...
PMID:A special class of non-histone protein tightly complexed with template-inactive DNA in chromatin. 114 2

DNA- and RNA-concentrations, as well as in vitro activities of DNase I (EC 3.1.4.5), DNase II (EC 3.1.4.6), and DNase I inhibitor, have been determined in 63 spontaneous (man) and 22 experimentally induced (rat) nervous system blastomas of various types and of different degrees of malignancy. Generally, a distinct elevation of DNA concentrations and of the ratio (Q) of DNase II- to DNase I-activities has been observed when compared with control values. A statistically significant relationship could be demonstrated between increase of DNA concentrations and Q in experimentally induced neurinomas of rats as well as in human astrocytomas and glioblastomas. Whereas the increase of Q may be a biochemical expression of elevated DNA synthesis of tumour cells, no conclusions can be drawn as to the role of DNases in the process of malignant transformation.
 ...
PMID:[Deoxyribonucleases in spontaneous and experimental tumors of the nervous system]. 118 37

For studying the mechanism of hyperoxia toxic effect on metabolism in the rat brain localization of lysosomes enzymes - acid phosphatase, DNase II and acid peptid-hydrolases were investigated in the brain subcellular fractions under different phases of oxygen poisoning and in the in vitro experiments. Under hyperoxia redistribution of the lysosome enzymes is found between the fraction enriched with lysosomes and the soluble one. The character of redistribution evidences for disturbance of permeability in the brain lysosome membranes under hyperoxia. Urea possessing a protective effect under these conditions prevents from labilization of lysosome enzymes which is evoked by the effect of oxygen hyperoxia. When studying manifestation of the effect of lysosome hydrolases release on the substrate level there were found constancy of DNA content in the brain under hyperoxia and a decrease in polymeric property of the brain DNA an hour after the beginning of the terminal phase of oxygen poisoning.
 ...
PMID:[Lysosome enzymes of brain in hyperoxia and under the effect of urea]. 120 6

Effect of different concentration of non-ionic detergents (Triton X-100, Triton X-305, BRIJ-35 and Triton WR-1339) on total and non-sedimentable activity of 8 rat liver lysosome enzymes (acid phosphatase, acid DNase, acid RNase, arylsulphatases A and B, beta-glucuronidase, beta-galactosidase, beta-glucosidase and beta-acetylglucosaminidase) was studied. Only Triton X-100 at the concentration of 0.1% (and higher) was found to release completely lysosome enzymes. Low concentrations of Triton X-100 (0.025-0.05%) were used to characterize the strength of enzyme binding: the level of releasing acid DNase, beta-galactosidase, beta-glucuronidase and acid phsophatase being considerably higher than that of other lysosome enzymes studied. On the basis of the data obtained a method is worked out, which is suitable for series studies of the stability of lysosome membranes under different physiological and pathological conditions. The essence of the method is the treatment of membrane particles with increasing concentrations of Triton X-100 (0.025; 0.05 AND 0.1%) AND THE SUCCESSIVE ESTIMATION OF NON-Sedimentable activity of marker enzymes. The method detected troubles in the stability of rat liver lysosome membranes under starvation, protein deficiency and aging.
 ...
PMID:[Determination of lysosome membrane stability]. 120 72

By means of isopycnic centrifugation in the continuous density gradient of sucrose two subfractions of lysosomes were isolated from rat liver homogenates: a "light" one (with the floating density p=1.13) and a "heavy" one (p=1.24). Electron microscopic, enzymatic and electron microscope enzymatic analysis of the isolated subfractions showed that the "light" subfraction consisted mainly of newly-formed primary lysosomes, while the "heavy" one was presented by secondary lysosomes. Parallel biochemical investigations demonstrated a considerable enzymatic heterogeneity of the two lysosomal subfractions: the "light" subfraction was characterized by a high specific activity of acid DNase, acid RNase and beta-galactosidase, and by almost total absence of beta-glucosidase activity, while the "heavy" one was characterized by a high specific activity of beta-glucosidase, beta-glucuronidase and beta-N-acetylglucosaminidase. Possible causes of enzyme heterogeneity of rat liver lysosomes are discussed.
 ...
PMID:[Morphologic and biochemical heterogeneity of lysosomes]. 123 Oct 99

5838-DNI, an inhibitor of deoxyribonuclease (DNase) II from porcine spleen was produced by Streptomyces sp. strain No. A-5838. The structure of 5838-DNI was shown to be 1,4,4a,5,12,12a-hexahydro-4,4a,11,12a-tetrahydroxy-3,8-dimethoxy-9- methoxycarbonyl-10-methyl-1,5,12-trioxo naphthacene. Although similar in structure to tetracenomycin C, which is an antibiotic against Gram-positive bacteria, 5838-DNI has different antibacterial activity. 5838-DNI was distinguished from 5923-DNI, a previously reported DNase II inhibitor, in inhibitory activity against each enzyme. 5838-DNI showed dependency of inhibition on pH and temperature, and inhibited phosphodiesterase I in a competitive manner. These data suggest that 5838-DNI is the first reported example of an inhibitor of microbial origin which is able to inhibit DNase II and phosphodiesterase I.
 ...
PMID:5838-DNI, a deoxyribonuclease inhibitor produced by Streptomyces sp. strain no. A-5838. 128 32

After electrophoresis in DNA-containing polyacrylamide gels, two acid DNase activities can be detected in peripheral, mononuclear cells of the human blood. One of these acid DNase activities correlates with cell proliferation; its isoelectrical point is at pI 7.4. By means of this DNase activity, a quantity of less than 1% leukemic cells can be detected. The increased acid DNase activity can indicate the proliferation of malignant cell populations and possibly the proliferation of cell populations during immunological reactions.
 ...
PMID:Acid DNase activities in peripheral, mononuclear blood cells: a possible parameter to detect proliferating cell populations. 128 30


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>