Year: 2015
Type: article
Abstract: The presence of a dehydrin-like protein in buckwheat seeds had been revealed using an antibody against a Lysrich conservative motif sequence for dehydrin.In this study, the dehydrin protein was purified from a Japanese variety of buckwheat seed (Fagopyrum esculentum cv.Kitawase) through four purification steps: heat treatment, addition of 10-45% saturated ammonium sulfate, ion-exchange chromatography on a HiTrap Q Fast Flow column, and gel filtration on a HiPrep Sephacryl S-200 column.Results of peptide mapping with trypsin indicated that the purified protein contained conservative motif sequences and Gly-rich sequences, which are characteristic to dehydrin proteins.The results of the pepsin digestion experiment showed that the purified dehydrin was promptly cleaved by simulated gastric fluid, and that a 16-kDa polypeptide that is highly resistant to pepsin digestion was produced.
DOI: 10.24514/00002944
Author: M. Momma
Language: Japanese
Subfield: Plant Science
Domain: Life Sciences
SDG: Zero hunger
Open Access status: green
OpenAlex ID: W979478183