Novel enzymatic properties of DNA-Pt complexes.
DNA-Pt complexes have shown novel enzymatic activity as a peroxidase similar to that of horseradish peroxidase in the colorimetric reaction with its substrate. The enzymatic activity of these complexes increased with increasing reaction time and pH in reaction solutions of DNA and K2[PtCl4]. This enhanced enzymatic activity was attributed to the increase in Pt conjugated to DNA in the complex. The enzymatic activity per unit mole of the DNA-Pt complex was significantly higher for complexes prepared with high molecular weight DNA because the enzymatic activity of the complex per repeat unit of DNA was almost constant for these complexes prepared under the same reaction conditions. All the DNA-Pt complexes in this study prepared with different DNA sequences (i.e., [A]20, [G]20, [C]20, [T]20, and [AG]10) exhibited peroxidase enzymatic activity. These complexes showed good thermal stability as compared to native horseradish peroxidase.
Matsuoka
Yuki
Y
Department of Materials and Life Science, Seikei University, 3-3-1 Kichijoji Kitamachi, Musashino, Tokyo 180-8633, Japan.
Onodera
Toru
T
Kojima
Toshinori
T
Chang
Yung
Y
Chen
Wen-Yih
WY
Imanaka
Takanobu
T
Fukushima
Hisashi
H
Higuchi
Akon
A
D000818:Animals; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004795:Enzyme Stability; D009944:Organoplatinum Compounds / Q000737:chemistry* / Q000378:metabolism; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism*; D010984:Platinum / Q000737:chemistry*; D012474:Salmon
D009944:Organoplatinum Compounds; D010984:Platinum; D004247:DNA; D010544:Peroxidases