A comparison of the initiating abilities of ribo- and deoxyriboprimers in DNA polymerization catalyzed by AMV reverse transcriptase
| Autor: | G. A. Nevinsky, I.A. Lokhova, Gorn Vv, M V Repkova, Olga I. Lavrik, N.K. Rudenko, V.M. Kavsan, A.G. Veniaminova |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
DNA Replication
Stereochemistry Polynucleotides Biophysics Biology Biochemistry chemistry.chemical_compound Structure-Activity Relationship Km for primer Structural Biology Genetics AMV reverse transcriptase Molecular Biology chemistry.chemical_classification Avian Myeloblastosis Virus DNA replication RNA-Directed DNA Polymerase Cell Biology Templates Genetic Molecular biology Reverse transcriptase Kinetics Enzyme chemistry Polymerization Polynucleotide Nucleic acid Primer (molecular biology) DNA |
| Zdroj: | FEBS Letters. (1-2):156-158 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(90)81352-O |
| Popis: | The difference in optimal conditions for DNA polymerization catalyzed by AMV reverse transcriplase on poly(A) and poly(dA) templates with d(pT)10 and (pU)10 primers has been found. A comparison of the initiating abilities of d(pT)10 and (pU)10, primers under optimal conditions for various template · primer complexes has been made. The best template · primer complex was poly(A) · d(pT)10 and the worst was poly(A) · (pU)10. The lengthening of d (pT)n primers by a mononucleotide unit (n=2 10) increases their affinity by a factor of about 2 and 3 in the case of poly(dA) and poly(A) templates, respectively. The affinities ofd (pT)11–25 to the enzyme does not change with the primer length. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|