Norephedrines as metabolites of [14C]amphetamine in urine in man

(+/-)-[(14)C]Amphetamine sulphate (20mg) was administered orally to each of two human male subjects, and 80-85% of the (14)C was excreted in the urine in 2 days. The metabolites in the first day's urine were examined quantitatively. Apart from the metabolites previously described (Dring et al., 1970), norephedrine (2.2 and 2.6% of dose in the two subjects respectively) and 4-hydroxynorephedrine (0.3 and 0.4% of dose in the two subjects respectively) were also found.     

SUMO conjugation in plants

Covalent attachment of small proteins to substrates can regulate protein activity in eukaryotes. SUMO, the small ubiquitin-related modifier, can be covalently linked to a broad spectrum of substrates. An understanding of SUMOs role in plant biology is still in its infancy. In this review, we briefly summarize the enzymology of SUMO conjugation (sumoylation), and the current knowledge of SUMO modification in Arabidopsis thaliana (L.) Heynh. and other plants, in comparison to animals and fungi. Furthermore, we assemble a list of potential pathway components in the genome of A. thaliana that have either been functionally defined, or are suggested by similarity to pathway components from other organisms.     

Mechanism of conjugation

Summary A new conditional thermosensitive Hfr mutant of Escherichia coli K-12 was isolated. The ts mutation is cotransducible with purE and tsx loci on the E. coli chromosome. Upon temperature shift to 42° C the DNA synthesis and transfer of chromosome is stopped immediately and RNA, protein synthesis in about ten minutes.     

In vitro protein-polysaccharide conjugation: tyrosinase-catalyzed conjugation of gelatin and chitosan

The enzyme tyrosinase was used for the in vitro conjugation of the protein gelatin to the polysaccharide chitosan. Tyrosinases are oxidative enzymes that convert accessible tyrosine residues of proteins into reactive o-quinone moieties. Spectrophotometric and dissolved oxygen studies indicate that tyrosinase can oxidize gelatin and we estimate that 1 in 5 gelatin chains undergo reaction. Oxidized tyrosyl residues (i.e., quinone residues) can undergo nonenzymatic reactions with available nucleophiles such as the nucleophilic amino groups of chitosan. Ultraviolet/visible, (1)H-NMR, and ir provided chemical evidence for the conjugation of oxidized gelatin with chitosan. Physical evidence for conjugation was provided by dynamic viscometry, which indicated that tyrosinase catalyzes the sol-to-gel conversion of gelatin/chitosan mixtures. The gels formed from tyrosinase-catalyzed reactions were observed to differ from gels formed by cooling gelatin. In contrast to gelatin gels, tyrosinase-generated gels had different thermal behavior and were broken by the chitosan-hydrolyzing enzyme chitosanase. These results demonstrate that tyrosinase can be exploited for the in vitro formation of protein-polysaccharide conjugates that offer interesting mechanical properties.