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7
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0024828309
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Larsen T.A., Goodsell D.S., Cascio D., Grzeskowiak K., Dickerson R.E. J. Biomol. Struct. Dyn. 7:1990;477.
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(1990)
J. Biomol. Struct. Dyn.
, vol.7
, pp. 477
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Larsen, T.A.1
Goodsell, D.S.2
Cascio, D.3
Grzeskowiak, K.4
Dickerson, R.E.5
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8
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0025039741
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DAPI also interacts with G-C rich regions of duplex DNA by intercalation albeit the binding was 1000-fold weaker than its A-T rich minor groove binding. There is no fluorescence enhancement through this mode of interaction.
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1.
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(1990)
J. Histochem. Cytochem.
, vol.38
, pp. 1323
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Kapuscinski, J.1
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9
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0027022325
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Yamana K., Ohashi Y., Nunota K., Aoki M., Nakano H., Sangen O. Nucleic Acids Symp Ser. 27:1992;135.
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(1992)
Nucleic Acids Symp Ser.
, vol.27
, pp. 135
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-
Yamana, K.1
Ohashi, Y.2
Nunota, K.3
Aoki, M.4
Nakano, H.5
Sangen, O.6
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13
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85030949627
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-
note
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+), 429.1675.
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-
-
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14
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85030949816
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Fluorescence assay for DNA binding by DNA fluorescent dyes, compound 4 and DAPI (2): Separate stock solutions were made for the above DNA dyes in TE (10 mM Tris/1 mM EDTA, pH 7.5) buffer, respectively, at a concentration of 0.01 mg/mL. To a group of tubes that each contained 4 μg/mL of calf thymus DNA (CT-DNA) were added, respectively, appropriate amounts of a particular fluorescent dye stock solution in such a way that the resulting tubes contained the various ratios between CT-DNA and the dye as defined in Table 1. All resulting solutions were mixed well and, after incubated at room temperature for 10 min, each solution was measured on a fluorescence spectrometer with excitation at 358 nm and emission 461 nm. All results are summarized in Table 1
-
Fluorescence assay for DNA binding by DNA fluorescent dyes, compound 4 and DAPI (2): Separate stock solutions were made for the above DNA dyes in TE (10 mM Tris/1 mM EDTA, pH 7.5) buffer, respectively, at a concentration of 0.01 mg/mL. To a group of tubes that each contained 4 μg/mL of calf thymus DNA (CT-DNA) were added, respectively, appropriate amounts of a particular fluorescent dye stock solution in such a way that the resulting tubes contained the various ratios between CT-DNA and the dye as defined in Table 1. All resulting solutions were mixed well and, after incubated at room temperature for 10 min, each solution was measured on a fluorescence spectrometer with excitation at 358 nm and emission 461 nm. All results are summarized in Table 1.
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-
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15
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-
85030941193
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-
An 'ideal' DNA helix has 10 base pairs per turn
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An 'ideal' DNA helix has 10 base pairs per turn.
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-
-
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17
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-
85030953430
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-1
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-1.
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18
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85030940935
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3, respectively. After it was stirred at room temperature overnight, the reaction mixture was evaporated to dryness and the residue was taken up in about 50 mL of water and then filtered. The filtrate was separated on a Rainin preparative RP-HPLC system equipped with a Waters Delta-Pak C-18 cartridge column (4 inch diameter, 100 Å pore size, 15 μm particle size). The elution was effected with a gradient generated between 0.1% trifluoroacetic acid (TFA) in water and acetonitrile at a flow rate of 50 mL/min (Table 2
-
3, respectively. After it was stirred at room temperature overnight, the reaction mixture was evaporated to dryness and the residue was taken up in about 50 mL of water and then filtered. The filtrate was separated on a Rainin preparative RP-HPLC system equipped with a Waters Delta-Pak C-18 cartridge column (4 inch diameter, 100 Å pore size, 15 μm particle size). The elution was effected with a gradient generated between 0.1% trifluoroacetic acid (TFA) in water and acetonitrile at a flow rate of 50 mL/min (Table 2.
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-
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19
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85030944894
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note
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20 It was found that 91% of the available ε-amino groups of the BSA lysine residues were modified by 1.
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-
-
-
20
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0013935465
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The percentage of lysine modification was calculated by using the TNBS assay developed by Goldfarb and modified by Snyder and Sobocinski. (a) Goldfarb A.R. Biochem. 5:1966;2570 (b) Snyder S.L., Sobocinski P.Z. Anal. Biochem. 64:1975;284.
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(1966)
Biochem.
, vol.5
, pp. 2570
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Goldfarb, A.R.1
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21
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0016636179
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The percentage of lysine modification was calculated by using the TNBS assay developed by Goldfarb and modified by Snyder and Sobocinski. (a)
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The percentage of lysine modification was calculated by using the TNBS assay developed by Goldfarb and modified by Snyder and Sobocinski. (a) Goldfarb A.R. Biochem. 5:1966;2570 (b) Snyder S.L., Sobocinski P.Z. Anal. Biochem. 64:1975;284.
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(1975)
Anal. Biochem.
, vol.64
, pp. 284
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Snyder, S.L.1
Sobocinski, P.Z.2
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