@ARTICLE{Shevelev1998617,
author={Shevelev, I.V. and Legina, O.K. and Tutaev, K.Yu. and Krutyakov, V.M.},
title={Strong inhibition of endodeoxyribonucleases at physiological ionic strength},
journal={Molecular Biology},
year={1998},
volume={32},
number={4},
pages={617-620},
note={cited By 2},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032338570&partnerID=40&md5=009a39ba9d3ad1e3457b14fb608ba88c},
affiliation={Konstantinov Inst. of Nucl. Physics, Russian Academy of Sciences, Gatchina, 188350, Russian Federation},
abstract={Endonucleases were inhibited more than 100 times in the presence of 50 mM ammonium sulfate or other salts (NaCl, KCl, NH4Cl, KH2PO4, Na2SO4) at the same ionic strength at pH 7-9, while 3′→5′ exonuclease and DNA polymerase α were inhibited less than two times. The effect was similar with bovine pancreatic DNase I and various endonuclease preparations (cell extracts and purified enzymes from Drosophila melanogaster embryos, rat liver, rat spleen, rat brain gray substance, calf spleen, and calf thymus), regardless of the substrate (Escherichia coli native or denatured DNA, phage λ DNA, phage φX174 single-stranded circular DNA and its replicative forms). In vitro inhibition at nearly physiological salt concentrations (150-200 mM) explains the relatively low endonuclease activity in vivo and in cell extracts. DNA degradation during apoptosis can be due to a local decrease in ionic strength and, therefore, activation of cell endonucleases. Ionic strength inhibition of endonucleases allows exact estimation of the activity of various DNA enzymes (polymerases, helicases, topoisomerases, exonucleases, etc.) during their isolation and purification, and can be used to protect phage DNA in various experiments.},
author_keywords={Endodeoxyribonucleases;  Inhibition;  Ionic strength;  Physiological conditions},
correspondence_address1={Shevelev, I.V.; Konstantinov Inst. of Nucl. Physics, Russian Academy of Sciences, Gatchina, 188350, Russian Federation; email: igor@omrb.pnpi.spb.ru},
issn={00268933},
language={English},
abbrev_source_title={Mol. Biol.},
document_type={Article},
source={Scopus},
}

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Physics, Russian Academy of Sciences, Gatchina, 188350, Russian Federation","abstract":"Endonucleases were inhibited more than 100 times in the presence of 50 mM ammonium sulfate or other salts (NaCl, KCl, NH4Cl, KH2PO4, Na2SO4) at the same ionic strength at pH 7-9, while 3′→5′ exonuclease and DNA polymerase α were inhibited less than two times. The effect was similar with bovine pancreatic DNase I and various endonuclease preparations (cell extracts and purified enzymes from Drosophila melanogaster embryos, rat liver, rat spleen, rat brain gray substance, calf spleen, and calf thymus), regardless of the substrate (Escherichia coli native or denatured DNA, phage λ DNA, phage φX174 single-stranded circular DNA and its replicative forms). In vitro inhibition at nearly physiological salt concentrations (150-200 mM) explains the relatively low endonuclease activity in vivo and in cell extracts. DNA degradation during apoptosis can be due to a local decrease in ionic strength and, therefore, activation of cell endonucleases. Ionic strength inhibition of endonucleases allows exact estimation of the activity of various DNA enzymes (polymerases, helicases, topoisomerases, exonucleases, etc.) during their isolation and purification, and can be used to protect phage DNA in various experiments.","author_keywords":"Endodeoxyribonucleases; Inhibition; Ionic strength; Physiological conditions","correspondence_address1":"Shevelev, I.V.; Konstantinov Inst. of Nucl. Physics, Russian Academy of Sciences, Gatchina, 188350, Russian Federation; email: igor@omrb.pnpi.spb.ru","issn":"00268933","language":"English","abbrev_source_title":"Mol. Biol.","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Shevelev1998617,\r\nauthor={Shevelev, I.V. and Legina, O.K. and Tutaev, K.Yu. and Krutyakov, V.M.},\r\ntitle={Strong inhibition of endodeoxyribonucleases at physiological ionic strength},\r\njournal={Molecular Biology},\r\nyear={1998},\r\nvolume={32},\r\nnumber={4},\r\npages={617-620},\r\nnote={cited By 2},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032338570&partnerID=40&md5=009a39ba9d3ad1e3457b14fb608ba88c},\r\naffiliation={Konstantinov Inst. of Nucl. Physics, Russian Academy of Sciences, Gatchina, 188350, Russian Federation},\r\nabstract={Endonucleases were inhibited more than 100 times in the presence of 50 mM ammonium sulfate or other salts (NaCl, KCl, NH4Cl, KH2PO4, Na2SO4) at the same ionic strength at pH 7-9, while 3′→5′ exonuclease and DNA polymerase α were inhibited less than two times. 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