Results 221 to 230 of about 14,669 (270)

Deoxyribonuclease inhibitors

European Journal of Medicinal Chemistry, 2014
Deoxyribonucleases (DNases) are a class of enzymes able to catalyze DNA hydrolysis. DNases play important roles in cell function, while DNase inhibitors control or modify their activities. This review focuses on DNase inhibitors. Some DNase inhibitors have been isolated from various natural sources, such as humans, animals (beef, calf, rabbit and rat),
Ana, Kolarevic, Denitsa, Yancheva, Gordana, Kocic, Andrija, Smelcerovic   +3 more
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SIMPLIFIED ANTISTREPTOCOCCAL DEOXYRIBONUCLEASE ASSAY

Journal of Bacteriology, 1962
Olitzky, Irving(Bio-Science Laboratories, Los Angeles, Calif.),Sam Berkman, and Doris Bass. Simplified antistreptococcal deoxyribonuclease assay. J. Bacteriol.84:1011–1015. 1962.—A simple antistreptococcal deoxyribonuclease assay has been devised in which dilutions of the patient's serum are reacted with deoxyribonuclease, and residual active enzyme is
I, OLITZKY, S, BERKMAN, D, BASS
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Chromosome Breakage by Deoxyribonuclease

Nature, 1970
THE possibility that endogenous deoxyribonuclease might play a part in inducing chromatid breakage was suggested by our experiments describing a high incidence of chromosome breaks and rearrangements in human diploid cell strains after selective damage to lysosomes1.
G R, Paton, A C, Allison
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Rutin as Deoxyribonuclease I Inhibitor

Chemistry & Biodiversity, 2019
AbstractDNase I inhibitory potential of water extract of nine Hypericum species (H. umbellatum, H. barbatum, H. rumeliacum, H. rochelii, H. perforatum, H. tetrapterum, H. olympicum, H. hirsutum, H. linarioides) and the most important Hypericum secondary metabolites (hypericin, hyperforin, quercetin, and rutin) was investigated.
Ana Kolarevic, Aleksandra Pavlovic, Aleksandra Djordjevic, Jelena Lazarevic, Sasa Savic, Gordana Kocic, Marko Anderluh, Andrija Smelcerovic   +7 more
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DEOXYRIBONUCLEASES FROM RAT BRAIN*

Journal of Neurochemistry, 1968
Abstract—Two distinctly different DNases were isolated from rat brain and could be separated easily by ammonium sulphate fractionation. One of the DNases acts optimally at pH 5.0 hydrolysing preferentially native DNA and requiring an optimal Mg2+ concentration of about 0.03 m.
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Endo-deoxyribonuclease from Streptomyces rimosus

Applied Microbiology and Biotechnology, 1995
From filtrates of an oxytetracycline-producing culture of Streptomyces rimosus a deoxyribonuclease was purified to homogeneity and determined to be a potent endo-DNase. It is a monomeric, basic protein (M(r) approximately 21,000; pI approximately 9.5) stable in a broad pH range but unstable to higher temperature.
Vukelić, Bojana, Ritonja, Anka, Vitale, Ljubinka   +2 more
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Deoxyribonucleases in Human Parotid Saliva

Enzyme, 1975
Deoxyribonuclease (EC 3.1.4.5, EC 3.1.4.6) activities in human parotid saliva were examined by microdisc electrophoresis. Three fractions, differing in their electrophoretic mobility and in their optimal incubation conditions, were characterized. The various enzyme activities were tested at pH 5.0 in 100 mmol with l-minus 1 Na-acetate buffer or at pH 7.
E J, Zöllner, D M, Klepsch, R K, Zahn, R, Knepper   +3 more
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Deoxyribonuclease immobilized on the erythrocytes

Experientia, 1981
Bovine pancreatic deoxyribonuclease (DNase I) was immobilized on human erythrocytes with several procedures. DNase immobilized on the erythrocytes by chromic chloride showed DNase activity in vitro. Other binding procedures inhibit the immobilized DNase activity.
T, Kitao, Y, Kitao, K, Hattori
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Invertebrate acid deoxyribonucleases

Journal of Cellular and Comparative Physiology, 1964
A P, RUSSELL, D I, PATT, C, TERNER
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Multiple forms of deoxyribonuclease I

Molecular and Cellular Biochemistry, 1981
This article will review recent progress on the purification of DNase I (E.C.3.1.4.5) from various sources and the characterization of multiple forms of the enzyme. The chemical basis of the multiple forms in bovine pancreas will be discussed in detail, while for other DNases, including those in ovine pancreas, bovine, mouse and rat parotid, and malt ...
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