scholarly journals Activity of acid deoxyribonuclease towards diastereoisomers of thymidyl 3'-(4-nitrophenyl phosphorothioate). Stereochemistry of transnucleotidylation reaction.

1986 ◽  
Vol 261 (2) ◽  
pp. 592-598
Author(s):  
B Uznanski ◽  
W Niewiarowski ◽  
W J Stec
1975 ◽  
Vol 30 (11-12) ◽  
pp. 781-784 ◽  
Author(s):  
E. Jürgen Zöllner ◽  
Hans Störger ◽  
Hans-Joachim Breter ◽  
Rudolf Zahn

Abstract Deoxyribonucleases, Disc Electrophoresis, Lymphocytes Four groups of deoxyribonuclease activities from human lymphocytes have been characterized by deoxyribonuclease assay in DNA-containing polyacrylamide gels following their separation by disc-electrophoresis. All activities hydrolyse DNA endonucleolytically. One neutral deoxyribo­ nuclease found in the cytoplasmic fraction prefers native or UV-irradiated DNA over denatured DNA as substrate and is a 5′-monoester former. Two groups of acid deoxyribonuclease activities are detectable in the nuclear fraction. Both are 3′-monoester formers. One is as well active with denatured DNA as with native DNA, the other one shows the same activity with native and UV-irradiated DNA but lower activity with denatured DNA. An alkaline deoxyribonuclease activity, also localized in the nucleus, is a 5′ -monoester DNA as substrate.


Blood ◽  
1995 ◽  
Vol 86 (6) ◽  
pp. 2414-2418 ◽  
Author(s):  
RA Gottlieb ◽  
HA Giesing ◽  
RL Engler ◽  
BM Babior

Human neutrophils are terminally differentiated cells that spontaneously undergo apoptosis in tissue culture. Apoptosis in these cells can be delayed by culture in the presence of granulocyte colony- stimulating factor or other inflammatory mediators. Neutrophils were found to contain an acid endonuclease that appeared to be responsible for the internucleosomal DNA cleavage that accompanies apoptosis. As measured by a plasmid nicking assay, this endonuclease had a molecular weight (M(r)) of 35,000, a pH optimum of 5.5, and a threshold for activity of pH 6.6 to 6.8. It was weakly inhibited by divalent cations (Ca2+, Mg2+, and Zn2+) and more strongly inhibited by aurintricarboxylic acid and N-bromosuccinimide. DNA from neutrophils treated with nigericin in buffers of defined pH displayed nucleosomal ladders whose prominence varied with pH in a manner that paralleled the pH dependence of the plasmid cleavage assays, consistent with internucleosomal DNA cleavage by the acid endonuclease. We have previously shown that neutrophils undergo acidification to a pH value as low as 6.0 during apoptosis; we suggest that this endonuclease may be responsible for the DNA cleavage seen in apoptotic neutrophils.


1971 ◽  
Vol 147 (2) ◽  
pp. 728-733 ◽  
Author(s):  
Robert Townend ◽  
Giorgio Bernardi

1971 ◽  
Vol 26 (6) ◽  
pp. 589-594 ◽  
Author(s):  
K. Tempel

The behaviour of the in vitro-activities of an alkaline and an acid deoxyribonuclease (DNase I and II, resp.), and of an inhibitor of DNase I of the kidney of mice, as well as of the DNA- and protein-content of kidneys and thymus, was studied in about 500 mice 4 hours to 21 days after exposure to folic acid in doses of 60 — 180 mg/kg body-weight.The most important results can be summarized af follows:1. Activity of DNase I decreased and activities of DNase II and of a DNase I-inhibitor increased under the influence of high doses of folic acid. Significant effects were observed 16 — 24 hours after folic acid-injections. Extreme values (80% decrease [DNase I], 180% increase [DNase II, DNase I-inhibitor]) were reached after 2 and 4 days and were dose-dependent. Control values reappeared within 1 — 3 weeks.2. Protein- and DNA-content of the thymus behaved very similarly to DNase I-activity of the kidney.3. The increase of the DNase II-activity of the kidney under the influence of folic acid resulted from enzyme induction. As to the behaviour of DNase I loss of enzyme out of damaged cells and the induction of a DNase I-inhibitor in the kidney must be taken into account.4. In many systems DNase I may control DNA-synthesis. Preliminary studies on the behaviour of folic acid-induced reaction of the kidney, when inhibited by X-irradiation, Actinomycin D, Actidione, or poly (vinylsulfate), suggest that DNase I-inhibitor plays a certain role in combining protein- and DNA-synthesis by inhibiting DNase I.


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