Myristicin and elemicin are phenylallyl derivatives present in nutmeg. The similarity of their chemical structure to that of mescaline or certain amphetamine derivatives has led to the assumption that the psychotropic effect of nutmeg in man is due to amphetamine derivatives endogenously produced from these phenylallyl precursors by bio-transformation. In our present study we investigated the metabolism of myristicin by rat liver, using the isolated perfused liver or incubation of liver homogenate. We have experimentally proved for the first time that rat liver is capable of converting myristicin into 3-methoxy-4,5-methylenedioxyamphetamine (MMDA). Identification of MMDA was achieved by two-dimensional thin-layer chromatography of the dansylated amine and further by mass spectroscopy.

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The abuse of nutmeg for narcotic purposes has led to renewed chemical and pharmacological interest in this drug. Several allylbenzene derivatives whose biological transformation products have structures resembling mescaline and amphetamine have been identified as psychotropic constituents. It is suggested that the intensity of the hallucinogenic action of these compounds is due to the possibility of simulation of LSD-like structural elements.

Lectins have specificity for certain carbohydrate structures in macromolecules. Lectins are, therefore, useful histochemical tools for demonstrating the composition and localization of components of connective tissue matrices, such as articular cartilage. In order to assess the significance of observed lectin-binding patterns, experiments were performed in which monoclonal antibodies against chondroitin sulphate- and keratan sulphate-containing proteoglycans and link proteins were applied to sections of bovine articular cartilage after enzymatic digestion with chondroitinase ABC and keratanase. The following conclusions were made: (1) Binding of peanut agglutinin (PNA) in the interterritorial matrix predominantly indicates the presence of keratan sulphate, but may also detect O-linked oligosaccharides of proteoglycans. (2) In normal cartilage wheat germ agglutinin (WGA) binds nearly exclusively to keratan sulphate. In cartilage degraded with chondroitinase ABC and keratanase this lectin may also detect carbohydrates in link protein due to enhanced accessibility. Binding of WGA to O-linked oligosaccharides may eventually occur. (3) In enzymatically digested cartilage matrix, staining with soybean agglutinin (SBA) may be due to link protein, but not to chondroitin sulphate, because specific breakdown of the glycosaminoglycan chain is required for binding of SBA. (4) Ulex europaeus agglutinin I (UEA I) binding sites are only detectable in digested cartilage matrix.

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