[Determination of inhibition sites during hydrolysis of polydeoxyribonucleotides by exonucleases III from Bacillus amyloliquefaciens and Escherichia coli].
The influence of the primary structure of polydeoxyribonucleotides on the rate of hydrolysis with exonuclease III from Bacillus amyloliquefaciens and Escherichia coli was investigated. The substrates used were synthetic oligodeoxyribonucleotides and pBR 322 DNA fragments labeled with 32P at the 5'-termini of one of the chains. According to the data from polyacrylamide gel electrophoresis performed under denaturing conditions, the hydrolysis of these substrates by unsaturating concentrations of B. amyloliquefaciens and E. coli exonuclease III proceeds with several reproducible "stops". The decrease of the reaction rate was shown to take place just before the pyrimidine blocks in the digested DNA chain.
Chikaev
N A
NA
Nazarenko
I A
IA
Bogachev
S S
SS
Malygin
E G
EG
D001407:Bacillus / Q000201:enzymology; D001483:Base Sequence; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology; D005090:Exodeoxyribonucleases / Q000378:metabolism*; D006868:Hydrolysis; D011089:Polydeoxyribonucleotides / Q000378:metabolism*
D011089:Polydeoxyribonucleotides; D005090:Exodeoxyribonucleases; C020133:exodeoxyribonuclease III
Opredelenie uchastkov tormozheniia pri gidrolize polidezoksiribonukleotidov ékzonukleazami III iz Bacillus amyloliquefaciens i Escherichia coli.