✍ Scribed by Barbara Behr; Maria Biaŀowolska; Jerzy Chodkowski
No coin nor oath required. For personal study only.
The problem of the effect of proteins on electrode reactions has been discussed many times in the literature. In our previous paper 1 we briefly reviewed interpretations of the mechanism of inhibition given by various authors. Since that time there have appeared several papers related to this problem, most noteworthy being that by Holleck et al. 2.
These authors suggest that the charge on the protein molecule should influence its adsorption, depending on the electrode charge, and that this could be the cause of different inhibiting properties in neutral and acidic solutions.
However, they have found using a.c. polarographic methods that double layer capacity is lowered by gelatine throughout the whole potential range in acidic solutions also. The authors do not seem to know either the paper by Tanford 3, who has presented the most consistent interpretation of the effects of proteins on electrode reactions or those by Dratovsky and Ebert 4.
The variety of facts described in the literature on the inhibiting action of proteins does not allow any general conclusions to be easily drawn. However it seemed useful to get some more data especially on the double layer capacity of the mercury electrode in the presence of proteins in neutral and acidic solutions. The aim of this paper was also to perform some experiments to check the interpretation of Tanford 3, whose ideas had many features in common with those discussed by several other authors, sometimes independently, concerning different systems (e.g. ref. 5).
📜 SIMILAR VOLUMES
The orientation of coumarin molecqles adsorbed at a mercury surface depends on potential, coumarin concentration and ionic strength of the electrolyte. At positive potentials the adsorbed molecules are arranged with the plane of the ring parallel to the mercury surface; as the potential is made more