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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Characterization of the Bacteriophage ΦKMV DNA Ligase

Author(s): R. Lavigne, B. Roucourt, K. Hertveldt and G. Volckaert

Volume 12, Issue 7, 2005

Page: [645 - 648] Pages: 4

DOI: 10.2174/0929866054696127

Price: $65

Abstract

Gene 17 product (gp17) of the Pseudomonas aeruginosa-infecting bacteriophage phiKMV shows in silico similarity to T7 DNA ligase. In a semi-quantitative activity assay, it is shown that gp17 is a functional, ATP-dependent DNA ligase, in spite of some structural differences related to DNA-binding properties). Enzymatic activity of His6-based purified expression product was optimised (4°C at 24h for sticky end double-stranded DNA fragments) and estimated at 0.5 Weiss U/μg.

Keywords: dna ligase, bacteriophage, recombinant protein, phikmv


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