Characterization of a multi-functional metal-mediated nuclease by MALDI-TOF mass spectrometry | Zendy

Uraiwan Puapaiboon | Zendy

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Characterization of a multi-functional metal-mediated nuclease by MALDI-TOF mass spectrometry

Author(s) -

Uraiwan Puapaiboon

Publication year - 2001

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/29.17.3652

Subject(s) - nuclease , mass spectrometry , manganese , exonuclease , exonuclease iii , biology , enzyme , chromatography , biochemistry , chemistry , escherichia coli , polymerase , organic chemistry , gene

Mass spectrometric analysis of reaction products allows simultaneous characterization of activities mediated by multifunctional enzymes. By use of MALDI-TOF mass spectrometry, the relative influence of magnesium and manganese promoted exonuclease and phosphatase activities of Esherichia coli exonuclease III have been quantitatively measured, offering a rapid and sensitive alternative to radioactivity quantification and gel electrophoresis procedures for determination of reaction rate constants. Manganese is found to promote higher levels of exonuclease activity, which could be a source of mutagenic effects if this ion were selected as the natural cofactor. Several potential applications of these methods to quantitative studies of DNA repair chemistry are also described.

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