Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.21.3 (deoxyribonuclease)
1,528 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Electrophoretic cell separation by means of free-flow electrophoresis in an FF5 apparatus was investigated with respect to band resolution, separation capacity, reproducibility and influence on cell viability. Very sharp bands and a large separation capacity were achieved using triethanolamine/acetate buffered glycine media as liquid curtain. Acid buffer ions such as N-2-hydroxyethylpiperazine-N'-ethanesulfonic acid (HEPES) or phosphate produced broader bands. Osmotic expanders such as saccharides, though preserving cell viability excellently, decrease electrophoretic velocity and thus separation capacity. The decrease in cell viability observed in glycine media could be compensated for by addition of Ca2. Band broadening caused by methodologically specific velocity flow profiles could be reduced to a negligible level by coating the chamber walls with albumin and by appropriate adjustment of sample flow rate and liquid curtain velocity. Under the optimum conditions described, selective cell loss and artificial change in electrophoretic mobility of the cells during operation can be disregarded. The main reason for cell loss was cell aggregation at low ionic strength, which can be prevented or reversed by treatment of the cells with deoxyribonuclease.
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PMID:Free-flow electrophoresis. II. Analysis of the method with respect to preparative cell separation. 117 90

The recently isolated neutral deoxyribonuclease from crab (Cancer pagurus) testes has been characterized in its mode of action and its specificity. The enzyme is a typical endonuclease, forming 5'-phosphate oligonucleotides of large average size; after extensive digestion of calf thymus DNA over 75% of the fragments have a size larger than pentanucleotides and mononucleotides are absent. As far as specificity is concerned, thymidine is very abundant in the 5'-penultimate position (approximately 50%) and in the 3'-terminal position (37%) and almost absent in the 5'-terminal position (approximately 1%), the values quoted concerning Escherichia coli digests of average size (Pn) between 50 and 10.
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PMID:The specificity of a neutral deoxyribonuclease from Cancer pagurus. 123 41

Synthetic chocolate colourant, flavourant and the mixture of both were administered to healthy adult male albino rats to evaluate their effect on the nucleic acids metabolism, i.e. deoxyribonucleic and ribonucleic acids (DNA and RNA), total serum protein, thyroid hormones (T4 and T3) and nuclease enzymes, i.e. cytoplasmic- and mitochondrial deoxyribonuclease and ribonuclease (DNase and RNase) in brain, liver, and kidneys. Also, the activity of the fundamental enzymes of the oxidative pentose phosphate pathway, i.e. cytoplasmic and mitochondrial glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase (G-6-PD and 6-PGD), as well as total lipids and cholesterol contents in the same organs were studied. Ingestion of the studied food additives significantly increased serum protein, RNA and T4 hormone, while, DNA and T3 hormone were insignificantly elevated. In connection with this, the hydrolytic enzymes of nucleic acids (DNase and RNase activities) were stimulated by all studied food additives and in all mentioned organs. The activity of G-6-PD and 6-PGD in both cytoplasmic and mitochondrial fractions of all studied organs were increased. The highest increase was noticed in rats fed on diets supplemented with the mixture of both colourant and flavourant followed by colourant then flavourant, respectively.
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PMID:Biochemical effect of chocolate colouring and flavouring like substances on thyroid function and protein biosynthesis. 171 48

When isolated human fibroblast lysosomes are incubated with 4 microM [32P]phosphate at pH 7.0, orthophosphate is transported into lysosomes and is rapidly incorporated into low and high molecular weight products. We have characterized the high molecular weight (HMW) lysosomal material into which [32P]phosphate is incorporated and have found it to consist of long chains of inorganic polyphosphate based on the following observations. 1) greater than 97% of HMW 32P-lysosomal material is converted to [32P]orthophosphate when incubated with 1 N HCl for 20 min at 100 degrees C. 2) Incubation of HMW 32P-lysosomal material at pH 7.0 and 65 degrees C for 96 h results in the formation of [32P]trimetaphosphate, which is known to be produced only from linear chains of polyphosphate under these conditions. 3) HMW 32P-lysosomal material is resistant to degradation by proteinase K, ribonuclease, and deoxyribonuclease and extracts into the aqueous phase during phenol/chloroform extractions. 4) HMW 32P-lysosomal material displays heterogeneous mobility on polyacrylamide gels with most chains ranging in length from 100 to at least 600 phosphate residues. 5) HMW 32P-lysosomal material is partially hydrolyzed under alkaline conditions to yield a continuous ladder of polyphosphate species differing by one or several residues in length on polyacrylamide gels.
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PMID:Incorporation of [32P]orthophosphate into long chains of inorganic polyphosphate within lysosomes of human fibroblasts. 174 Apr 14

We previously demonstrated that pneumococcal extracts contain a highly specific inhibitor of human neutrophil elastase (HNE). We now show that the active inhibitor in these extracts is a high-molecular-weight, heat-stable substance that appears to be RNA, since inhibitory activity of pneumococcal extracts is decreased by incubation with ribonuclease but not by incubation with deoxyribonuclease or proteinase K. Moreover, metabolically labeled ([3H]uridine) pneumococcal RNA, isolated by phenol extraction followed by ethanol precipitation, strongly inhibits HNE. Pneumococcal capsular polysaccharide, although polyanionic, is only weakly inhibitory toward HNE and is not a major source of elastase-inhibitory activity in pneumococcal extracts. On the other hand, the capsule of Haemophilus influenzae type b contains polyribosylribitol phosphate. This highly charged polyanion possesses HNE-inhibitory activity, but only under special circumstances to be discussed below. Pneumococci (type I, type II smooth, type II rough) and H. influenzae (type b) all release HNE-inhibitory activity into their culture medium during growth. By contrast, Klebsiella pneumoniae and Staphylococcus aureus release little (if any) stable HNE-inhibitory activity during growth. We propose that some bacterial pneumonias may spare host tissue because polyanions released by the invading microorganisms (e.g. RNA from autolysing pneumococci) inhibit elastase released from inflammatory neutrophils and thereby modulate accompanying tissue proteolysis. Pneumonias caused by microorganisms that do not release stable polyanionic inhibitors of HNE (e.g., Staphylococcus and Klebsiella) may be correspondingly more injurious to the lung.
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PMID:Inhibition of human neutrophil elastase by bacterial polyanions. 244 47

The survival of several strains of Staphylococcus aureus after heat stress in different menstrua was not logarithmic and F-values were determined to express their resistance to heat. Of the strains tested, Staph. aureus 234 (enterotoxin B) was the most heat resistant and Staph. aureus 790 (enterotoxin E) was the most heat sensitive. Buffalo milk gave the best protection to all the strains of Staph. aureus against heat, followed by cow's milk; phosphate-buffered saline gave the least protection. Soyabean casein digest agar gave maximum recovery of survivors followed by brain heart infusion and Baird-Parker medium. At 50 degrees C there was no marked variation in coagulase production by the surviving strains but at 55 and 62.5 degrees C there was complete loss of coagulase activity. There was a decreased deoxyribonuclease (DNase) production by all the strains of Staph. aureus after heat stress. Heat-treatment at 55 and 62.5 degrees C resulted in loss of enterotoxin production by all the survivors except S6 and 234, the surviving cells of which still produced enterotoxin B after heat treatment at 55 degrees C. Most of the survivors regained lost characteristics such as coagulase, DNase and enterotoxin production after four to five passages through BHI which suggests that subculture of Staph. aureus recovered from heat-processed milk is necessary to avoid false results.
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PMID:Variation in the behaviour of enterotoxigenic Staphylococcus aureus after heat stress in milk. 249 81

A novel deoxyribonuclease, exonuclease V, has been purified approximately 30,000-fold from Saccharomyces cerevisiae. Exonuclease V is localized in the nucleus. The nuclease degrades single-stranded, but not double-stranded, DNA from the 5'-end. The products of exonuclease action are dinucleotides, except the 3'-terminal tri- and tetranucleotides which are not degraded. Studies with synthetic oligo- and polynucleotides with specified sequence elements showed that exonuclease V cleaves off dinucleotides as primary digestion products. Thus, the polymers (pT)9pA(pT)n and (pT)10pA(pT)n yielded pTpA and pApT as digestion products, respectively. Removal of the 5'-terminal phosphate from the DNA substrate results in reduced binding of the enzyme to the substrate. In addition, the initial hydrolytic cut by exonuclease V on the dephosphorylated substrate produces a mixture of dinucleoside monophosphates and trinucleoside diphosphates. The enzyme is processive in action.
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PMID:Exonuclease V from Saccharomyces cerevisiae. A 5'----3'-deoxyribonuclease that produces dinucleotides in a sequential fashion. 328 46

A method has been developed for the isolation of outer membranes from Acinetobacter sp. strain MJT/F5/199A. Washed cells were broken in a French press and, after deoxyribonuclease and ribonuclease treatment, removal of intact cells, and four washes in 20 mosmol phosphate buffer, pH 7.4, with centrifugation at 25,000 x g for 10 min, preparations of cell wall fragments from which almost all pieces of plasma membrane had been removed resulted. Treatment of the cell walls with lysozyme and further washing, in the presence of 20 mM MgCl(2), yielded preparations of outer membranes. Electron microscopy of freeze-etched preparations shows that a regular pattern of subunits is present on the outer surfaces of intact cells. After negative staining, these subunits are visible on isolated walls and outer membranes; they can be removed by brief treatment with papain. In section, the cell wall structure is that typical of gram-negative bacteria, but the subunits are not detectable on the surface of the outer membrane. The outer membrane retains the appearance of a "unit membrane" in the cell wall, isolated outer membrane, and papain-treated outer membrane fractions. Both cell walls and outer membranes contain a high percentage of protein (76 and 84%, respectively) and not more than 5% carbohydrate, of which glucose and galactose are constitutents. The outer membranes of this Acinetobacter thus differ in structure and composition from those of bacteria in the Enterobacteriaceae.
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PMID:Isolation of outer membranes with an ordered array of surface subunits from Acinetobacter. 412 37

An ATPase activity that is completely dependent on DNA is associated with the ATP-dependent DNase (recB-recC enzyme) purified from Escherichia coli. There is a strong correlation between the ATPase and the DNase activities under various assay conditions. With E. coli DNA as substrate, 8-9 molecules of ATP are hydrolyzed to ADP and inorganic phosphate for every phosphodiester bond hydrolyzed by the DNase. The possible functional relationship of the ATPase and DNase activities is discussed.
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PMID:Adenosine triphosphatase associated with adenosine triphosphate-dependent deoxyribonuclease (recB-recC enzyme-E. coli-ATP to phosphodiester hydrolysis ratio-DNA-dependent ATPase activity). 425 17

A protein kinase which is intimately associated with equine herpesvirus (equine abortion virus) was found by using adenosine triphosphate-gamma-(32)P as a phosphate donor and virus protein as an acceptor. Consistent demonstration of the activity requires prior removal of phosphohydrolase. The kinase activity requires Mg(2+), is not stimulated by cyclic adenosine monophosphate, but is enhanced by added protamine or arginine-rich histone. The labeled product is resistant to ribonuclease, deoxyribonuclease, and chloroform-methanol but is sensitive to Pronase. Other tests suggest that serine and threonine residues are the acceptor sites. In the in vitro reaction, the incorporation represents an average of approximately 4,500 phosphate residues per virion, and all 17 virus protein bands resolved by polyacrylamide gel electrophoresis appear to be labeled.
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PMID:Protein kinase activity in equine herpesvirus. 433 15


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