Hamablet, L., Chen, G. C., Brown, A., Roberts, R. J. (August 1989) LpnI, from Legionella pneumophila, is a neoschizomer of HaeII. Nucleic Acids Res, 17 (15). p. 6417. ISSN 0305-1048
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Abstract
Lpnl is a Type II restriction endonuclease that was previously isolated from Legionella pneumophila strain 11 EJ and partially purified (1). Further purification by phosphocellulose and DNA-agarose chromatography, with an intermediate 50-75% ammonium sulphate concentration/fractionation step gave enzyme sufficiently pure for detailed characterization. Lpnl cleaves pUC19 DNA at three sites. Double digests of pUC19 DNA with Lpnl and either AatXl, EcoRI, Pvul or Rsdl mapped the Lpnl cleavage sites to approximately 230, 690 and 1090 nucleotides. These sites lie close to those predicted for Haell. A double digest between Haell and Lpnl on bacteriophage X. DNA confirmed that these en/ymes are isoschizomers (
Item Type: | Paper |
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Uncontrolled Keywords: | Comparative Study DNA, Viral/metabolism Deoxyribonucleases, Type II Site-Specific/*metabolism Legionella/*enzymology Substrate Specificity |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing organs, tissues, organelles, cell types and functions > organs types and functions > metabolism organism description > virus |
CSHL Authors: | |
Communities: | CSHL labs > Roberts lab |
Depositing User: | Gail Sherman |
Date: | 11 August 1989 |
Date Deposited: | 26 Jul 2017 14:20 |
Last Modified: | 08 Nov 2017 16:57 |
PMCID: | PMC318316 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/34855 |
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