Paul Boquet

LOCALIZATION OF THE CHOLINERGIC RECEPTOR PROTEIN IN ELECTROPHORUS ELECTROPLAX 'BY HIGH RESOLUTION AUTORADIOGRAPHY

We first confirm that the [“HI o-toxin binds exclusively to the innervated (caudal) side of the eel electroplax and further show that the o-toxin binds both between the synapses and under the nerve terminals. However, taking into account the particular stereology of the cytoplasmic membrane, it appears that the density of a-toxin molecules bound per unit area of actual membrane surface is approx. 100 times larger under the synapses than outside the synapses. Absolute values of this density and of the total number of receptor sites per cell are given.

An attempt to classify the toxic proteins of elapidae and hydrophiidae venoms

Abstract Toxins recently extracted from Elapidae and Hydrophiidae venoms are chemically closely related basic proteins of low molecular weight. They fall into three main serological groups. Their classification is based on the results of precipitation tests.

LOCALIZATION OF THE CHOLINERGIC RECEPTOR PROTEIN BY IMMUNOFLUOROSCENCE IN EEL ELECTROPLAX

noninnervated, face does not receive nerve endings, is not excitable, but is specialized in the active trans- port of sodium and potassium. As expected from their different functions, the cytoplasmic membranes which limit these two faces differ by their enzyme content. As shown both

Studies of tubocurarine labelled with iodine or tritium

Summary D-tubocurarine was reacted first with ICl and then with tritium by catalytic hydrogenolysis of the iodo derivative in the presence of tritium gaz. The specific radioactivity of the tritiated product reached 12 Ci/mmole and its biological activity was identical to that of the original material. From the iodinated material (0.8 atom per mole) pure monoiodo-d-tubocurarine was obtained by selective adsorption on a Biogel column. Localization of the halogen was characterized by pKs measurements of the two phenolic functions of the iodo and of the original d-tubocurarine. Circular dichroism spectra and toxicity measurements of the iodinated compound have shown that iodine does not, or very slightly only, modify the structural and biological properties of d-tubocurarine.

Antigénicité et pouvoir immunogène des toxines extraites des venins d'Elapidae et d'Hydrophiidae

In this article the results are reported of recent experiments concerning the antigenicity and the immunogenic properties of some basic toxic proteins recently extracted from snake venoms. A serological classification of these substances is proposed. 3 groups have now been determined. As most of the low molecular weight proteins (<10.000) the immunogenicity of the α toxin ofNaja nigricollis, taken as an example, is poor. The influence of polymerization of this toxin, and the adjuvant effect of the Freund mixture on the production of specific antibodies, are described. By affinity chromatography, using Sepharose 4B as a carrier, antibodies against this toxin were separated from the other proteins of the antiNaja nigricollis horse immune-serum. They belong to the IgT immunoglobulins. By the same technique, when erabutoxin ‘a’ fromLaticauda semifasciata is covalently linked to the Sepharose, antibodies reacting with both this toxin and the α toxin were separated from the same immuneserum. This confirms that an immunological relationship exists between the α toxin of an Elapidae:Naja nigricollis, and the erabutoxin ‘a’ of an HydrophiidaeLaticauda semifasciata.