Abstract
Changes in peptides and their amino-acid composition that take place during the plastein reaction carried out with immobilizedα-chymotrypsin as a catalyst and with the low-molecular weight peptide fraction of alfalfa (Medicago sativa) leaf protein hydrolyzate as substrate were studied. By thin-layer fingerprint chromatography the substrate and the plastein reaction product exhibited five and six peptide species, respectively. The analysis of their amino-acid composition indicated that the substrate peptides in two cases gave rise to plastein peptides by slight apparent compositional changes, in the other cases instead they underwent more pronounced modifications.
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