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pubmed-article:9055038pubmed:abstractTextThe stability of stereoregular oligo(nucleoside phosphorothioate)s (PS-oligos) in human plasma has been studied. 3'-Exonuclease present in human plasma appeared to be RP specific, that is, it cleaves internucleotide phosphorothioate linkages of [RP]-configuration and not those of [SP]-configuration. Therefore, PS-oligos containing all phosphorothioate internucleotide linkages of [RP]-configuration [RP-PS-oligos]) are more effectively degraded by the enzyme than PS-oligos prepared via nonstereo-controlled methods (so-called random mixture of diastereomers [Mix-PS-oligos]), whereas oligo(nucleoside phosphorothioate)s of [S(P)]-configuration remain intact. The enzyme activity depends on the sequence of nucleobases. The presence of deoxycytidine units (three or more residues) at the 3'-end of PS-oligo substrate significantly inhibits the enzyme activity.lld:pubmed
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pubmed-article:9055038pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9055038pubmed:year1997lld:pubmed
pubmed-article:9055038pubmed:articleTitleStability of stereoregular oligo(nucleoside phosphorothioate)s in human plasma: diastereoselectivity of plasma 3'-exonuclease.lld:pubmed
pubmed-article:9055038pubmed:affiliationPolish Academy of Sciences, Department of Bioorganic Chemistry, Lód?, Poland.lld:pubmed
pubmed-article:9055038pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9055038pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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