The DNA primase of Sulfolobus solfataricus is activated by substrates containing a thymine-rich bubble and has a 3'-terminal nucleotidyl-transferase activity. [electronic resource]
Producer: 20041015Description: 5223-30 p. digitalISSN:- 1362-4962
- Adenosine Triphosphate -- metabolism
- DNA -- chemistry
- DNA Primase -- isolation & purification
- Enzyme Activation
- Enzyme Stability
- Hydrogen-Ion Concentration
- Nucleotidyltransferases -- metabolism
- Oligodeoxyribonucleotides -- chemistry
- Oligoribonucleotides -- biosynthesis
- Poly T -- chemistry
- RNA -- biosynthesis
- Substrate Specificity
- Sulfolobus -- enzymology
- Templates, Genetic
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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