✍ Scribed by Eugène Fredericq
No coin nor oath required. For personal study only.
The influence of serum albumin, ovalbumin and insulin on the absorption spectra of organic anions in solution is investigated in the visible range. The spectra of azo-dyes, phthaleins, indigosulphonates and anthraquinone dyes are affected in the same way by the three proteins: there is a general depression of the intensity of absorption and slight shifts of the maximum. Moreover the modifications are similar to those produced by 90yb aqueous dioxane. These facts are interpreted by Van der Waals interactions between hydrophobic parts of dyes and proteins.
On the contrary the spectra of picrate and flavianate ions are differently affected by 90% dioxane and by serumalbumin. In the latter case there is a marked shift towards shorter wave lengths indicating a diminution of the resonance. This is interpreted by the formation of hydrogen bonds between proteins and nitro-groups. The spectral study confirms the deductions previously made on the nature of interactions between proteins and anions.
On sait depuis longtemps que le spectre de divers anions organiques est profondement alter6 en presence de certaines proteines a faible concentration. On a a plusieurs reprises attire I'attention sur l'influence que presente ce phenomene pour la determination du pH par les indicateurs colores en presence de proteines.
Klotz (l) a montre qu'il y avait une corrklation directe entre ces modifications e t le degre d'association des ions colores e t des proteines : 1. a y-globuline et la gklatine qui ne fisent pas ( l ) I. M. KLOTZ,
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