Polynucleotide Ligase-Catalyzed Joining of Deoxyribo-oligonucleotides on Ribopolynucleotide Templates and of Ribo-oligonucleotides on Deoxyribopolynucleotide Templates*†
AUTOR(ES)
Kleppe, K.
RESUMO
T4 polynucleotide ligase efficiently catalyzes the head-to-tail joining of the ribo-oligoadenylates, r-(pA)8 and r-(pA)10, in the presence of high molecular weight deoxypolythymidylate. The enzyme also catalyzes the joining of deoxy-oligothymidylates, e.g., d-(pT)10, in the presence of ribopolyadenylate. The enzyme failed to bring about the joining of r-(pA)10 when poly r-U was used as the template, although a slow formation of the expected activated intermediate from r-(pA)10 was detected.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=283168Documentos Relacionados
- Enzymatic synthesis of deoxyribo-oligonucleotides of defined sequence. Deoxyribo-oligonucleotide synthesis*
- Enzymatic synthesis of deoxyribo-oligonucleotides of defined sequence. Properties of the enzyme*
- Synthesis and NMR study of ribo-oligonucleotides forming a hammerhead-type RNA enzyme system.
- SYNTHETIC DEOXYRIBO-OLIGONUCLEOTIDES AS TEMPLATES FOR THE DNA POLYMERASE OF ESCHERICHIA COLI: NEW DNA-LIKE POLYMERS CONTAINING REPEATING NUCLEOTIDE SEQUENCES*
- Thermodynamic and kinetic studies of the formation of triple helices between purine-rich deoxyribo-oligonucleotides and the promoter region of the human c-src proto-oncogene.