Figure 1. Possible pathways for the reduction of sulfate to cysteine.
Figure 2. General structure of glucosinolates
Figure 3. The biosynthesis of glucosinolates.
Figure 4. Products of glucosinolate degradation by myrosinase.
Figure 5. SDS-PAGE of fractions with halide/bisulfide methyltransferase activity from the successive steps of purification.
Figure 6. Elution of the halide/bisulfide methyltransferase from a Protein Pak Q column upon anion exchange high performance liquid chromatography.
Figure 7. Elution of halide/bisulfide methyltransferase isoforms from a Protein Pak Q column upon anion exchange HPLC.
Figure 8. Elution of halide/bisulfide methyltransferase from an adenosine-agarose affinity column.
Figure 9. Elution of halide/bisulfide methyltransferase from a Superdex-75 HiLoad gel filtration HPLC column.
Figure 10. SDS-PAGE analysis of proteins at different steps of isoform purification.
Figure 11. Effect of pH on halide/bisulfide methyltransferase activity.
Figure 13. Effect of substrate concentration on the activity of the purified, pooled isoforms of halide/bisulfide methyltransferase.
Figure 15. Product inhibition kinetics of halide/bisulfide methyltransferase reaction with respect to S-adenosyl-L-methionine (AdoMet).
Figure 16. Product inhibition kinetics of halide/bisulfide methyltransferase reaction with respect to iodide, presented as double reciprocal plots.
Figure 17. Reaction mechanism of the halide/bisulfide methyltransferase.
Figure 18. Phase microscopy of chloroplast preparations.
Figure 19. HPLC profile of peptide fragments from tryptic digestion of the halide/bisulfide methyltransferase.
Figure 20. Matrix-assisted laser desorption mass spectrum of one tryptic fragment (P77) of the halide/bisulfide methyltransferase.
Figure 21. Similarity in amino acid sequence between the halide/bisulfide methyltransferase and other proteins.
Figure 22. Northern blot analysis of the halide/bisulfide methyltransferase transcript.
Figure 23. Degradation of indole glucosinolates by myrosinase.