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Lysine is an essential amino acid normally present in very low concentration in cereal seeds. In previous reports we have studied the metabolism of lysine in several distinct high-lysine maize mutants and observed drastic variations in the activity of saccharopine dehydrogenase (SDH), a key enzyme involved in lysine degradation. We have now analyzed the activity of SDH using non-denaturing polyacrylamide gel electrophoresis (PAGE) to identify possible isoenzymes that could explain the patterns of activity previously observed. The results indicated the presence of at least two SDH isoenzymes, one contributing to approximately 90% of the total enzyme activity and a minor form only present in the wild type lines and the opaque-1 mutant. The results suggest that the differences in total SDH activity among the genotypes tested are due to alterations in the predominant SDH isoenzymic form, which is likely to be the bifunctional polypeptide containing lysine 2-oxoglutarate reductase.

Barley (Hordeum vulgare L.) has had an important impact on human nutrition. Hull-less barley is a genetically improved type that has been widely used in recent years. Six Brazilian hull-less barley varieties (IAC-IBON 214-82; IAC 8612-421; IAC 8501-31; IAC 8501-12; IAPAR 39-ACUMAI; IAC 8501-22) were analyzed for storage protein constituents, amino acid contents, and similarity among the hull-less barley varieties. Albumins, globulins, prolamins I and II, and glutelins were extracted and separated by SDS-PAGE. The total protein amino acid contents of the flour were also determined for each variety by TLC and HPLC. Variations in intensity and appearance and disappearance of protein bands were observed among the varieties suggesting genetic variability. However, the amino acid profile did not indicate any major variations in the amino acid concentrations. The high lysine and threonine total concentrations detected in the seeds of the hull-less barley varieties encouraged an investigation into the re...