Slow rate of phosphodiester bond formation accounts for the strong bias that taq DNA polymerase shows against 2′,3′-dideoxynucleotide terminators

Biochemistry

Volumn 35, Issue 7, 1996, Pages 2189-2200

  Brandis, John W ^a   Edwards, Sydney G ^b   Johnson, Kenneth A ^b  

^a PERKINELMER INC   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DEOXYRIBONUCLEOTIDE; DNA POLYMERASE; NUCLEOTIDE DERIVATIVE; OLIGODEOXYNUCLEOTIDE;

ARTICLE; BACTERIOPHAGE T7; COMPLEX FORMATION; DISSOCIATION CONSTANT; DNA SEQUENCE; ENZYME KINETICS; ENZYME PURIFICATION; ESCHERICHIA COLI; MOLECULAR CLONING; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; STEADY STATE; THERMOSTABILITY; THERMUS AQUATICUS;

BASE SEQUENCE; DEOXYRIBONUCLEOTIDES; DNA-DIRECTED DNA POLYMERASE; ESTERIFICATION; KINETICS; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TAQ POLYMERASE;

EID: 0030051173     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi951682j     Document Type: Article

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