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Magenta green

Properties Red, blue, black, magenta, green colors avail. water-based disp. (48 02% act.) or powd. (> 88% act.) 97% < 6 m particle size pH 5.0-5.5 (disp.)... [Pg.187]

Printers use colored materials, eg, inks (qv), that absorb or subtract regions of the visible spectmm from white light. Subtractive color is usually represented by the three printer s primaries cyan, magenta, and yeUow (CMY). Cyan absorbs red light, magenta absorbs green, and yeUow absorbs blue light. [Pg.34]

The triaryknethane dyes are broadly classified into the triphenyknethanes (Cl 42000—43875), diphenylnaphthyknethanes (Cl 44000—44100), and miscellaneous triphenylmethane derivatives (Cl 44500—44535). The triphenyknethanes are classified further on the basis of substitution in the aromatic nuclei, as follows (/) diamino derivatives of triphenylmethane, ie, dyes of the malachite green series (Cl 42000—42175) (2) triamino derivatives of triphenylmethane, ie, dyes of the fuchsine, rosaniline, or magenta series (Cl 42500—42800) (J) aminohydroxy derivatives of triphenylmethane (Cl 43500—43570) and (4) hydroxy derivatives of triphenylmethane, ie, dyes of the rosoHc acid series (Cl 43800—43875). Monoaminotriphenyknethanes are known but they are not included in the classification because they have Httie value as dyes. [Pg.267]

Green-sensitized sliver halide layer Metallized magenta dye developer layer Spacer... [Pg.497]

Figure 14.15 Stmcture of the SI fragment of chicken myosin as a Richardson diagram (a) and a space-filling model (b). The two light chains are shown in magenta and yellow. The heavy chain is colored according to three proteolytic fragments produced by trypsin a 25-kDa N-terminal domain (green) a central 50-kDa fragment (red) divided by a cleft into a 50K upper and a 50K lower domain and a 20-kDa C-terminal domain (blue) that links the myosin head to the coiled-coil tail. The 50-kDa and 20-kDa domains both bind actin, while the 25-kDa domain binds ATP. [(b) Courtesy of 1. Rayment.]... Figure 14.15 Stmcture of the SI fragment of chicken myosin as a Richardson diagram (a) and a space-filling model (b). The two light chains are shown in magenta and yellow. The heavy chain is colored according to three proteolytic fragments produced by trypsin a 25-kDa N-terminal domain (green) a central 50-kDa fragment (red) divided by a cleft into a 50K upper and a 50K lower domain and a 20-kDa C-terminal domain (blue) that links the myosin head to the coiled-coil tail. The 50-kDa and 20-kDa domains both bind actin, while the 25-kDa domain binds ATP. [(b) Courtesy of 1. Rayment.]...
Fast sulphon black F ( C.I.26990). This dyestuff is the sodium salt of 1-hydroxy-8-( 2-hydroxynaphthylazo) -2- (sulphonaphthylazo) -3,6-disulph onic acid. The colour reaction seems virtually specific for copper ions. In ammoniacal solution it forms complexes with only copper and nickel the presence of ammonia or pyridine is required for colour formation. In the direct titration of copper in ammoniacal solution the colour change at the end point is from magenta or [depending upon the concentration of copper(II) ions] pale blue to bright green. The indicator action with nickel is poor. Metal ions, such as those of Cd, Pb, Ni, Zn, Ca, and Ba, may be titrated using this indicator by the prior addition of a reasonable excess of standard copper(II) solution. [Pg.319]

Fig. 2.8 Active site of NS3 protease with the inhibitor BILN 2061 added through molecular modelling [92], highlighting residues found to be mutated in resistance studies (Ala-156 and Asp-168, yellow Arg-155, green Gln-80, magenta). Fig. 2.8 Active site of NS3 protease with the inhibitor BILN 2061 added through molecular modelling [92], highlighting residues found to be mutated in resistance studies (Ala-156 and Asp-168, yellow Arg-155, green Gln-80, magenta).
Second, one dye-making process often led to others. Chemists learned to vary their recipes, as cooks do in kitchens. Treating magenta with other chemicals, for example, produced purples, blues, or greens. Accustomed to testing and analyzing compounds, chemists were now synthesizing them too. [Pg.23]

Figure 1. Relief maps of the electron density of (a) SCI2 and (b) H2O in the plane of the nuclei (density and distances from the origin of the coordinate system in au). Isodensity contour lines are shown in the order 0.001,0.002,0.004,0.008 (four outermost contours) 0.02,0.04,0.08 (next three) 0.2,0.4,0.8 (next three). The density is truncated at 2.00 au (innermost contour). These contours are shown in blue, violet, magenta, and green, respectively, on the figure in the table of contents (p 1028). Figure 1. Relief maps of the electron density of (a) SCI2 and (b) H2O in the plane of the nuclei (density and distances from the origin of the coordinate system in au). Isodensity contour lines are shown in the order 0.001,0.002,0.004,0.008 (four outermost contours) 0.02,0.04,0.08 (next three) 0.2,0.4,0.8 (next three). The density is truncated at 2.00 au (innermost contour). These contours are shown in blue, violet, magenta, and green, respectively, on the figure in the table of contents (p 1028).

See other pages where Magenta green is mentioned: [Pg.116]    [Pg.369]    [Pg.68]    [Pg.369]    [Pg.471]    [Pg.136]    [Pg.55]    [Pg.55]    [Pg.116]    [Pg.369]    [Pg.68]    [Pg.369]    [Pg.471]    [Pg.136]    [Pg.55]    [Pg.55]    [Pg.107]    [Pg.34]    [Pg.331]    [Pg.414]    [Pg.414]    [Pg.467]    [Pg.467]    [Pg.469]    [Pg.470]    [Pg.471]    [Pg.474]    [Pg.478]    [Pg.479]    [Pg.480]    [Pg.487]    [Pg.496]    [Pg.505]    [Pg.505]    [Pg.428]    [Pg.349]    [Pg.294]    [Pg.295]    [Pg.277]    [Pg.544]    [Pg.283]    [Pg.989]    [Pg.268]    [Pg.287]    [Pg.782]    [Pg.6]    [Pg.14]    [Pg.15]    [Pg.21]    [Pg.157]   
See also in sourсe #XX -- [ Pg.55 ]




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