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Titlebook: Enzymes of Molecular Biology; Michael M. Burrell Book 1993 Humana Press 1993

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https://doi.org/10.1007/978-1-4842-2102-0ed), reverse transcriptases (EC 2.7.7.49, RNA-dependent DNA polymerases that utilize an RNA template), and terminal deoxynucleotidyl transferases (EC 2.7.7.31, which require no template). This chapter will consider only DNA-dependent DNA polymerases (EC 2.7.7.7, DNA nucleotidyltransferases, DNA-directed).
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https://doi.org/10.1007/978-3-662-57305-1e N. or 5-C position of dC (EC 2.1.1.73) depending on the particular enzyme (.). The reaction is predominantly irreversible. Enzymes, such as ..-methylguanine DNA Mtase, that participate in DNA repair processes will not be discussed here.
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https://doi.org/10.1007/978-3-658-42460-2 located in many organs, including bone marrow, kidney, placenta, and intestinal mucosa), but have not been isolated from higher plants. The most commonly used alkaline phosphatases (AP) are those from calf intestinal mucosa (called CIAP, CIP, or CAP) and from the bacterium . (BAP).
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The BAL 31 Nucleases (EC 3.1.11),e shown (.,.) to be bacterial products. Only 10–20% of the nuclease activity is found in the periplasm (.). The American Type Culture Collection strain of . (ATCC 29659) produces BAL 31 nuclease as proficiently as the strain originally obtained from its discoverer.
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Pronase (EC 3.4.24.4),used, for example, to reveal the protein components of cell organelles by the hydrolysis of tissue slices (.), and as an alternative to proteinase K to remove protein during plasmid DNA (.), chromosomal DNA (.), and RNA isolation (.–.). Another use of pronase is the production of a protein hydrolysate suitable for amino acid analysis (.,.).
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