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)

A protein extracted and partially purified (about 100-fold) from mouse liver is able to inhibit the acid DNases from different tissues and species, whereas pancreatic DNase and E. coli endonuclease I are not inhibited. The acid DNase displays typical Michaelis-Menten kinetics in the absence of this inhibitor, but the kinetics become sigmoidal in its presence. The existence of a DNase-inhibitor complex is demonstrated by physicochemical experiments. Moreover, the inhibitor is able to reactivate the DNase treated by urea, probably through a reassociation of the inactive monomers to a dimeric state. An allosteric model in which the DNase-inhibitor complex is composed of catalytic (DNase) and regulatory (inhibitor) subunits could explain these data.
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PMID:A protein inhibitor of acid deoxyribonucleases. 490 93

A method for analyzing free nucleotides in the epidermis of the guinea pig is presented. Free nucleotides were extracted by using a methylalethanol mixture, and the analysis was carried out by high-pressure liquid chromatography on a column of Lichrosorb-NH2 with a single buffer of potassium phosphate. The concentration of total free nucleotides in the epidermis is about 4 times greater than that in the liver, kidney, spleen, or intestinal epithelium.l The free nucleotide level is markedly elevated in the hyperkeratotic epidermis induced by n-hexadecane. The alternation of free nucleotides in hyperkeratotic epidermis is discussed in relation to nucleic acid content, DNase, disc-electrophoretic properties of DNase, and salvage pathway enzymatic activity. Significant increases in the enzyme activity of the salvage pathway and in neutral DNase were observed in the hyperkeratotic stage. However, the DNA content and acid DNase activity were decreased. It is suggested that the pool size of free nucleotides in the epidermis is affected by the salvage enzyme system.
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PMID:High-pressure liquid chromatography of free nucleotide patterns in normal and abnormal keratinocytes. 616 23

The effect of early postnatal undernutrition and subsequent rehabilitation on wet weight, DNA, RNA, protein, and the activities of acid and alkaline DNases in white and grey matter region of rat brain was studied. In respect to the various parameters studied, white matter was found to be markedly vulnerable to undernutrition, but the grey matter region was unaffected. It has also been observed that the earlier the initiation of nutritional rehabilitation (10th postnatal day) the better was the recovery of the white matter to a normal condition, and in some cases early nutritional rehabilitation resulted in better than normal biochemical composition of the region. The specific activity of acid DNase was unaffected by weaning undernutrition in both white and grey matter. The total activity of this enzyme, which was significantly reduced in white matter of undernourished animals, exhibited a remarkable recovery following rehabilitation, to more than normal levels at 150 days of age. Total activity of alkaline DNase was reduced only in 15-day-old white matter of deprived animals, and here also rehabilitation brought back this enzyme to significantly more than normal levels. It is concluded that the two DNases, whatever their actual physiological role might be, are synthesized in a preferential manner during the rehabilitation.
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PMID:Differential effects of early undernutrition in white and grey matter regions of rat brain. 618 3

The effect of methylnitrosourea (MNU) on cerebellar and cerebral DNA, RNA, protein, lysosomal enzymes (acid DNase, RNase, phosphatase, and beta-glucuronidase), and 2',3'-cyclic nucleotide 3'-phosphohydrolase (2',3'-CNPase) activities was studied in rats from birth through 12 days of age. Subcutaneous injection of MNU in a dose of 0.625 mmol/kg caused a suppression of increase in weights and content of DNA, RNA, and protein of cerebellum, but no changes in those of the cerebrum or in body weight. Ratios of protein and RNA to DNA were substantially elevated by MNU in the cerebellum but not in the cerebrum. Acid DNase and acid RNase activities of MNU-treated rats were significantly elevated beyond the increase of these activities in controls in the cerebellum, but no change in these activities by MNU was observed in the cerebrum. A slight elevation in acid phosphatase activity was observed in the cerebellum but not in the cerebrum after MNU pretreatment. Beta-glucuronidase and 2',3'-CNPase activities were not changed in the cerebellum or in the cerebrum. These results suggest that in the developing brain, especially in the cerebellum at the mitotic stage, MNU caused cell damage and inhibited cell mitosis.
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PMID:Cytotoxic effects of methylnitrosourea on developing brain. 619 99

Acid deoxyribonuclease (EC 3.1.4.6) (DNase) from young (16 days of incubation) and old (1.5 years) chick cerebral hemispheres was purified to apparent homogeneity. Throughout the purification schedule, the behavior of "young" and "old" enzymes was similar. However, the specific activity of the purified enzyme from old brain was only one-tenth that of young enzyme. Polyacrylamide gel electrophoresis of the purified acid DNase gave a single band. Antisera against both "young" and "old" enzyme were raised and double immunodiffusion experiments revealed cross-reaction of young antigen with old antiserum and vice versa, although precipitin bands with young antigen against young antiserum and old antigen against old antiserum were more sharp. Both young and old acid DNase preparations showed an apparent molecular weight of 62,000 and many other properties like heat stability, effect of various exogenous compounds like Hg2+, Zn2+, Mg2+, etc., were also similar. The old enzyme showed slightly higher Km and decreased Vmax compared with the young enzyme. Dansylation of N-terminal amino acids and their analysis following tryptic digestion of both "young" and "old" acid DNase revealed a similar pattern. Immunotitration experiments showed that the old enzyme requires more antiserum prepared against "young" enzyme to achieve 50% inactivation, thus pointing out the presence of completely or partially inactive molecules in "old" acid DNase preparation. Circular dichroism spectra of the enzyme preparations indicated that the "old" acid DNase molecules are more rigid and have more alpha-helical structure, compared with the "young" enzyme. From these data, it is suggested that the reduction in the specific activity of old acid DNase may be, apart from other possibilities, due to conformational changes in the enzyme molecules.
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PMID:Age-dependent conformational changes in acid deoxyribonuclease of chick brain. 619 64

We studied DNA metabolism (synthesis and degradation) in brain to investigate the effect of hyperphenylalaninemia induced in rats by treatment with PCPA or alpha MPA plus PHE during suckling (4th-20th days of postnatal age) on cell proliferation and naturally occurring cell death. The incorporation of 14C in DNA as percent of total radioactivity in the tissue, 30 min after administration of [14C]thymidine served as a measure of DNA synthesis in vivo, and the amount of radioactivity recovered in DNA as percent of total 14C in the tissues of 21 day old rats, injected with [14C]thymidine on 2nd day after birth, indicated the turnover (degradation) of DNA. The results showed that the DNA content of cerebellum as well as cerebrum was reduced by treatment with PCPA plus PHE, while treatment with alpha MPA plus PHE had no effect on DNA content in cerebellum but reduced the levels in cerebrum. Treatment with PCPA or alpha MPA plus PHE reduced the synthesis of DNA in cerebrum of 11 day old rats but not in 21 day old rats, and the treatments did not affect DNA synthesis in cerebellum of either 11 or 21 day old rats. The turnover (degradation) of DNA was increased in both cerebellum and cerebrum from rats treated with PCPA plus PHE but alpha MPA plus PHE treatment did not alter the DNA turnover either in cerebellum or in cerebrum. The activity of acid DNase was reduced in both cerebellum and cerebrum from 11 as well as 21 day old rats treated with PCPA plus PHE, but the enzyme activity was not altered in the tissues from rats of both ages treated with alpha MPA plus PHE. The data thus indicate that in rats treated with PCPA plus PHE the reduction in cerebral DNA levels occurs due to reduced synthesis and/or increased turnover (degradation) of DNA but that the reduction in cerebellar DNA may occur only as a result of increased turnover (degradation), and that in rats treated with alpha MPA plus PHE the reduction in cerebral DNA must occur due to reduced synthesis. This suggests that treatment of rats with PCPA plus PHE during suckling inhibits cell proliferation and/or increases naturally occurring cell death in both cerebellum and cerebrum while treatment with alpha MPA plus PHE inhibits only cell proliferation and in cerebrum alone.
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PMID:Effect of hyperphenylalaninemia induced during suckling on brain DNA metabolism in rat pups. 623 57

Bloodstream forms of Trypanosoma brucei have been screened for the presence of enzymes that could serve as markers for the plasma membrane, flagellar pocket, lysosomes, endoplasmic reticulum and Golgi apparatus in order to study the subcellular organization of the digestive system of the parasite. Acetylesterase, acid DNase, acid phosphatase, acid phosphodiesterase, acid proteinase, acid RNase, alanine aminotransferase, galactosyl transferase, alpha-glucosidase, inosine diphosphatase and alpha-mannosidase were partially characterized and their assays optimized for pH-dependent activity, linearity of reaction with respect to incubation time and enzyme concentration, and the effect of inhibitors and activators. The association of these enzymes with particulate material and the presence of structural latency were investigated. Acid proteinase and alpha-mannosidase are particle-bound and latent in cytoplasmic extracts; they can be activated and solubilized in part by Triton X-100. Similar results were obtained for acid phosphatase, acid phosphodiesterase and inosine diphosphatase. Neutral alpha-glucosidase, though partly sedimentable, does not show latency and is readily solubilized by the detergent. Galactosyl transferase is firmly membrane-bound even in the presence of 0.1% Triton X-100. Cell fractionation by differential centrifugation and density equilibration on sucrose gradients revealed that both alpha-mannosidase and acid proteinase are associated with organelles that band at a density of about 1.20 g/cm3. Inosine diphosphatase, galactosyl transferase, acid phosphatase and acid phosphodiesterase sediment predominantly as microsomal constituents equilibrating at densities between 1.13 and 1.15 g/cm3. In addition, inosine diphosphatase and galactosyl transferase exhibit considerable activity at higher densities (1.18-1.25 g/cm3). Neutral alpha-glucosidase is mainly recovered in the nuclear and microsomal fraction; its particulate part equilibrates as a single band at rho = 1.22 g/cm3. Acetylesterase and acid DNase are largely soluble, whereas acid RNase does not produce distinct sedimentation and banding profiles. In intact cells, neutral alpha-glucosidase and acid phosphatase appear to be highly accessible to their substrates. It is tentatively concluded that (a) acid proteinase and alpha-mannosidase are lysosomal enzymes, (b) acid phosphatase and acid phosphodiesterase are associated with the flagellar pocket and part of the former enzyme probably with the endoplasmic reticulum, (c) galactosyl transferase is a constituent of the Golgi apparatus, and (d) alpha-glucosidase may serve as a marker for the plasma membrane. Inosine diphosphatase may also be derived from the latter structure.
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PMID:Subcellular fractionation of Trypanosoma brucei bloodstream forms with special reference to hydrolases. 624 76

Under conditions of three-hour hypobaric hypoxia the total activity of acid phosphatase and DNase in the rat liver somewhat lowers. The activity of free enzymes increases by 27 and 37%, and that of bound ones decreases by 42 and 24 %, respectively. Cytochrome c being introduced to hypoxic animals, the total activity of the enzymes does not significantly change. Under these conditions the activity of free acid phosphatase increases by 16%, and bound one decreases by 24 %. The activity of free acid DNase somewhat rises (by 12%) and that of bound one lowers (by 15%). A preliminary administration of cytochrome c to the organism prevents the development of pronounced changes in the activity of the studied lysosomal enzymes in the liver under grave hypoxia.
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PMID:[Effect of cytochrome c on the activity of lysosomal enzymes in the rat liver under hypobaric hypoxia]. 627 Aug 55

The total and unsedimentable activity of acid DNase, RNase, phosphatase and arylsulfatases A and B was examined in the rat kidneys during long-term compression of soft tissues in the presence of high excitability of the sympathoadrenal system. Injection of adrenalin to rats with trauma reduced the total activity of DNase, acid phosphatase and arylsulfatases A and B, particularly at the late periods of soft tissue compression, whereas the total activity of acid RNase slightly increased as compared with control. Compression of soft tissues after adrenalin preinjection was accompanied by a substantial rise of unsedimentable activity of the lysosomal enzymes under study in the kidneys. The activity of the enzymes in cytosol progressively ascended as the time of soft tissue injury increased.
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PMID:[Effect of adrenaline on kidney lysosome function in rats during prolonged soft tissue crushing]. 649 22

Primate liver lysosomal acid DNase is an endonucleolytic enzyme. The enzyme has both 3'- and 5'-nucleotidohydrolase activities. The oligonucleotides produced by DNase are polymers mainly about 30 mononucleotides long. The Arrhenius plot shows a discontinuity with a transition temperature at 47 degrees C, with an activation energy of 107 kJ/mol below and 67 kJ/mol above this temperature. The activation enthalpy is 104 kJ/mol and the entropy -0.498 kJ/mol/K. The enzyme is subject to substrate inhibition and the Km value is 159 X 10(-3) mM DNA-P.
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PMID:Lysosomal acid deoxyribonuclease from vervet monkey livers--II. Enzymic properties. 653 8


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