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Electrochemical assay for deoxyribonuclease I activity
Analytical Biochemistry, 2008A thiolated oligonucleotide having three ferrocenes was immobilized on a gold electrode through the sulfur-gold linkage. This electrode showed a current response based on the redox reaction of the ferrocene moieties and this response was decreased after treatment with deoxyribonuclease I (DNase I), suggesting the disappearance of the ferrocene moieties
Shinobu, Sato +6 more
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Multiple forms of deoxyribonuclease I
Molecular and Cellular Biochemistry, 1981This 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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Cell Biophysics, 1994
A number of phosphodiesterases, some of which possess additional biological activities (e.g., antitumor, immunosuppressive, and so on), have been considered for use in targeted tumor therapy. We propose Deoxyribonuclease I (DNase I), a compact, monomeric enzyme, as a very attractive candidate for targeting to tumor cells.
H, Linardou +3 more
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A number of phosphodiesterases, some of which possess additional biological activities (e.g., antitumor, immunosuppressive, and so on), have been considered for use in targeted tumor therapy. We propose Deoxyribonuclease I (DNase I), a compact, monomeric enzyme, as a very attractive candidate for targeting to tumor cells.
H, Linardou +3 more
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Radiation Research, 1962
The kinetic properties of irradiated deoxyribonuclease in aqueous solution were determined. They show that the maximum velocity and the Michaelis- Menten constant decreased with increasing radiation dose. The D/sub 37/ doses of the irradiated enzyme assayed at the low substrate concentrations were higher than those at the high substrate concentrations.
S, OKADA, G, FLETCHER
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The kinetic properties of irradiated deoxyribonuclease in aqueous solution were determined. They show that the maximum velocity and the Michaelis- Menten constant decreased with increasing radiation dose. The D/sub 37/ doses of the irradiated enzyme assayed at the low substrate concentrations were higher than those at the high substrate concentrations.
S, OKADA, G, FLETCHER
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Genetic polymorphism of human urine deoxyribonuclease I
Human Genetics, 1989A genetic polymorphism of human urine deoxyribonuclease I (DNase I) has been detected by the technique of polyacrylamide gel isoelectric focusing (IEF-PAGE) followed by immunoblotting with anti-DNase I antibody. Family studies showed that the three common phenotypes - DNASE1 1, 1-2, and 2 - and the other four rare phenotypes - DNASE1 1-3, 2-3, 2-4, and
K, Kishi, T, Yasuda, S, Awazu, K, Mizuta
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Fluorometric Determination of Deoxyribonuclease I Activity with PicoGreen
Analytical Biochemistry, 2000A rapid and sensitive assay for the detection of deoxyribonuclease I (DNase I) activity is described. This method is based on the ability of PicoGreen dye to enhance its fluorescence when bound to double-stranded DNA. In the standard assay, reaction mixtures containing the DNase I sample and 0.2 microg of the substrate DNA were prepared in a ...
S J, Choi, F C, Szoka
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Late Deoxyribonuclease Activity ofSalmonella enteritidis
American Journal of Clinical Pathology, 1979As a result of chance observations, the authors studied for deoxyribonuclease activity 16 strains of Salmonella, including six fresh isolates and ten stock cultures, with positive results in 13. Reactions characteristically occurred at 48 hours or later, with the majority being manifest at 72 hours and the latest at six days. No other positive reaction
M, Tomasulo, H, Braunstein
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1971
Publisher Summary This chapter discusses the chemical nature of deoxyribonuclease I (DNase I). A characteristic aspect of the kinetics of DNase I acting on native DNA is autoretardation. Autoretardation is caused by the continuous formation of products, which are poorer substrates than those from which they are derived.
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Publisher Summary This chapter discusses the chemical nature of deoxyribonuclease I (DNase I). A characteristic aspect of the kinetics of DNase I acting on native DNA is autoretardation. Autoretardation is caused by the continuous formation of products, which are poorer substrates than those from which they are derived.
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Deoxyribonuclease I Phenotyping from Saliva Stains
Journal of Forensic Sciences, 1999Abstract Good typing results were obtained using a newly developed method for extraction and purification of deoxyribonuclease I (DNase I) from saliva stains. Previously, DNase I phenotyping from saliva stains has been unsuccessful because of low enzyme activity and heavy contamination.
R, Iida +6 more
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Characterization of Preferred Deoxyribonuclease I Cleavage Sites
Journal of Molecular Biology, 1994The preferred DNase I cleavage sites within the 160 bp tyrT DNA fragment were identified by studying the initial rate of cleavage of individual bonds. The results show that there is no correlation between the rate of cleavage and the identity of the dinucleotide sequence that is cleaved.
J E, Herrera, J B, Chaires
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