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PubMed1976

[Drug-protein interactions: physico-chemical study on the interactions between chlorpromazine and glutamate dehydrogenase].

The molecular basis of inhibition of glutamate dehydrogenase by chlorpromazine was studied by circular dichoroism, differential spectroscopy and fluorescence. Chlorpromazine appears to induce conformational changes of the enzyme at the position of aromatic amino acids, and tryptophan residues in particular are involved. On the other hand the secondary structure of the enzyme is not influenced by binding of the drug.

Binding Sites↗
PubMed1975

Interactions of the third component of complement (C3) with cross-linked dextran. III. Isolation and characterization of interacting components after enzymatic digestion of complement coated cross-linked dextran.

In previous investigations we could show that incubation of cross-linked dextran (Sephadex) with normal human and normal guinea pig serum results in the binding of C3 to Sephadex. This binding was found to be due to activation of C3 via an alternate pathway. In this paper data are presented which show that components bound to Sephadex can be recovered after enzymatic digestion of serum-reacted Sephadex beads. The digests were characterized with immuno-electrophoresis and double immunodiffusion techniques. It could be shown that the main component present in the digest was converted C3. Apart from C3 under our test conditions only minute amounts of C3A but no other serum proteins were detectable. The observation that almost exclusively C3 is bound to Sephadex is further supported by the finding that immunization of rabbits with serum-reacted Sephadex beads results in the exclusive formation of anti C3 antibodies. Implications from these findings and possible applications are discussed.

Antibody Formation↗