Results 221 to 230 of about 170,315 (251)
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Active Site of Deoxyribonuclease I: I. The Nature of Active Site of Deoxyribonuclease I
Radiation Research, 1961Ionizing radiation and specific inhibitors for amino acid residues were used to demonstrate which amino acid residues are involved in the active site of the enzyme deoxyribonuclease I. Bromoacetic acid, lodoacetic acid, diisopropylfluorophosphate, p-chloromercuribenozate, tryptophan, histidine, cinnamic alcohol, cinnamaldehyde, indole, arginine, and ...
S, OKADA, G L, FLETCHER
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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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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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Benzimidazoles as novel deoxyribonuclease I inhibitors
Journal of Cellular Biochemistry, 2018AbstractInhibitory potential of 19 benzimidazoles against bovine pancreatic deoxyribonuclease I (DNase I) was investigated in vitro. Three compounds inhibited DNase I with IC50 below 100 μM and proved to be more potent DNase I inhibitors than crystal violet (IC50 = 351.82 ± 29.41 μM), used as a positive control.
Ana Kolarević +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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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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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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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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Depolymerization of F-actin by deoxyribonuclease I
Cell, 1976Deoxyribonuclease I causes depolymerization of filamentous muscle actin to form a stable complex of 1 mole DNAase I:1 mole actin. The regulatory proteins tropomyosin and troponin bind to filamentous actin and slow down but do not prevent the depolymerization. In the absense of ATP, heavy meromyosin binds tightly to actin filaments and blocks completely
S E, Hitchcock, L, Carisson, U, Lindberg
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Comparative biochemical properties of vertebrate deoxyribonuclease I
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2012Deoxyribonuclease I (DNase I, EC 3.1.21.1) is an endonuclease that preferentially attacks double-stranded DNA in a Ca(2+)-dependent manner to produce oligonucleotides with 5'-phospho and 3'-hydroxy termini. This review deals with the biochemical properties and molecular evolution of DNase I. A comparative study of vertebrate DNase I from Chondrichthyes
Junko, Fujihara +4 more
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