Hydrolysis of the 5′-p-nitrophenyl ester of TMP by oligoribonucleases (ORN) from Escherichia coli, Mycobacterium smegmatis, and human

Protein Expression and Purification

Volumn 57, Issue 2, 2008, Pages 180-187

  Young Park, Ah ^a   Elvin, Christopher M ^b   Hamdan, Samir M ^a   Wood, Robert J ^a   Liyou, Nancy E ^b   Hamwood, Tamarind E ^b   Jennings, Phil A ^b   Dixon, Nicholas E ^a,c  

^a AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

^b CSIRO   (Australia)

^c UNIVERSITY OF WOLLONGONG   (Australia)

Author keywords

3 5 exonuclease; DEDDh; Oligoribonuclease; RNA degradation; Spectrophotometric assay

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; GAMMAPROTEOBACTERIA; MYCOBACTERIUM SMEGMATIS;

EXORIBONUCLEASE; HIS HIS HIS HIS HIS HIS; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; HYBRID PROTEIN; NITROPHENOL; OLIGOPEPTIDE; OLIGORIBONUCLEASE; PROTEIN SUBUNIT; THYMIDINE PHOSPHATE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; GEL CHROMATOGRAPHY; HUMAN; HYDROLYSIS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR GENETICS; MYCOBACTERIUM SMEGMATIS; SEQUENCE ALIGNMENT; SOLUBILITY;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, GEL; ESCHERICHIA COLI; EXORIBONUCLEASES; HISTIDINE; HUMANS; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM SMEGMATIS; NITROPHENOLS; OLIGOPEPTIDES; PROTEIN SUBUNITS; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SOLUBILITY; THYMIDINE MONOPHOSPHATE;

EID: 37349051026     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.10.005     Document Type: Article

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