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Volumn 35, Issue 50, 1996, Pages

Interactions of the RecBCD enzyme from Escherichia coli and its subunits with DNA, elucidated from the kinetics of ATP and DNA hydrolysis with oligothymidine substrates

(2) Chamberlin, Mihaela a,b Julin, Douglas A a

a Bldg 142 (United States)

b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; HELICASE; NUCLEASE; OLIGONUCLEOTIDE; PROTEIN SUBUNIT; SINGLE STRANDED DNA; THYMIDINE DERIVATIVE;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME PURIFICATION; ESCHERICHIA COLI; HYDROLYSIS; MICHAELIS MENTEN KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; STEADY STATE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; DNA; ENDODEOXYRIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; EXODEOXYRIBONUCLEASE V; EXODEOXYRIBONUCLEASES; KINETICS; MACROMOLECULAR SUBSTANCES; MODELS, CHEMICAL; OLIGODEOXYRIBONUCLEOTIDES; SUBSTRATE SPECIFICITY;

EID: 4243127118 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi961643n Document Type: Article

Times cited : (8)

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