Table I. Trivial names of some glucosinolates with the corresponding side chain (R) composition.
Table II. Purification of the first anion exchange peak of halide/bisulfide methyltransferase.
Table III. Purification of H/BMT isoforms from 500 g of Brassica oleracea leaf tissue.
Table IV. Effects of -SH group inhibitors on the I- methylation activity of halide/bisulfide methyltransferase.
Table V. A survey of potential substrates for the halide/bisulfide methyltransferase.
Table VI. Methylating activity of the halide/bisulfide methyltransferase against various organic thiols and other analogous substrates.
Table VII. Effect of different methyl donors on the I- methylation activity of H/BMT.
Table VIII. Effect of different methyl donors on the I- methylation activity of the halide/bisulfide methyltransferase.
Table IX. Product inhibition kinetics for H/BMT isoforms.
Table X. Activity of H/BMT as compared to the rates of 14CO2 fixation and lipid synthesis in various chloroplast fractions.
Table XI. Activity of H/BMT as compared to those of marker enzymes after differential centrifugation.
Table XII. A survey of higher plants showing the association of the halide/bisulfide methyltransferase activity with the presence of glucosinolates.
Table XIII. Amino acid composition of three internal tryptic digests of isoform V of the halide/bisulfide methyltransferase.