Non-proteic immunogenic impurity in proteins purified by preparative electrophoresis on Pevikon.

Purified IgA proteins, obtained by zonal electrophoresis on blocks of Pevikon, contained an uncharged, non-proteic, water-soluble macromolecular impurity. The contaminant, which precipitates in half-saturated ammonium sulfate, could be an unknown derivative of polyvinyl alcohol. It was discovered because it induced the synthesis of specific precipitating antibodies in a rabbit used for antibody production against the electrophoresed protein, generating spurious precipitin reactions during its immunochemical analysis. Thorough washing of the Pevikon will substantially reduce the amount of impurity and the danger of obtaining precipitating antibodies against it after injection into animals.

Particle counting immunoassay. IV. The use of F(ab')2 fragments and N epsilon-chloroacetyl lysine N-carboxyanhydride for their coupling to polystyrene latex particles.

Improved performance with the latex agglutination immunoassay, PACIA, is possible when the F(ab')2 fragments of antibody are chemically coupled at their hinge region to a protein-coated latex using a new coupling reagent, N epsilon-chloroacetyl lysine N-carboxyanhydride. This reagent, whether by orientating the complete antibody molecule or its F(ab')2 fragment or by preventing antibody denaturation, increased the sensitivity of the PACIA method. The use of F(ab')2 fragments eliminated most serum interference with the test.

Phenyl-substituted normethadones: synthesis and pharmacology.

Phenyl-substituted normethadone derivatives were synthesized and their affinity (IC50) for opioid receptors was determined by displacement of the specific binding sites of [3H]sufentanyl on rat brain preparations. Substitution resulted in a decrease of affinity in-vitro. These results suggest that normethadone-like compounds may interact with the P subsite of the mu-opioid receptor and that the P subsite has a well-defined cavity shape of stringent dimensions.