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pubmed-article:6089795pubmed:abstractTextWhen nascent DNA of SV40 pulse labeled with [alpha-32p]dCTP in a permeable cell system was treated in situ with diisopropylfluorophosphate (DFP), a significant fraction of radioactivity was found to be covalently complexed with proteins. The adduct formation was demonstrated by density separation in CsCl, selective precipitation of the complexed DNA with SDS-KC1, and visualization of cross-linked proteins after SDS-PAGE. No cross-linking occurred with mature SV40 chromatin labeled in vivo and extracted from nuclei of infected cells. The DFP-induced DNA-protein cross-linking reaction appears to involve the protein's sulfhydryl groups since pretreatment with some sulfhydryl reagents completely inhibited the reaction.lld:pubmed
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