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.
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Claims 3
Claim · model-written summary
Purified buckwheat seed dehydrin contained conservative motif sequences and Gly-rich sequences by peptide mapping.
- Taxon
- Fagopyrum esculentum
Fagopyrum esculentume1 - Material
- cv.Kitawasee1
- Organ / stage
- seede1
- Gene
- dehydrin proteine1
- Outcome
- conservative motif sequences and Gly-rich sequencese2
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e1“dehydrin protein was purified from a Japanese variety of buckwheat seed (Fagopyrum esculentum cv.Kitawase)”
e2“Results of peptide mapping with trypsin indicated that the purified protein contained conservative motif sequences and Gly-rich sequences”
Claim · model-written summary
Purified dehydrin was promptly cleaved by simulated gastric fluid in a pepsin digestion experiment.
- Taxon
- Fagopyrum esculentumFagopyrum esculentume1
- Treatment
- pepsin digestione3
- Gene
- dehydrine3
- Outcome
- promptly cleavede3
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e1“dehydrin protein was purified from a Japanese variety of buckwheat seed (Fagopyrum esculentum cv.Kitawase)”
e3“The results of the pepsin digestion experiment showed that the purified dehydrin was promptly cleaved by simulated gastric fluid”
Claim · model-written summary
A 16-kDa polypeptide produced from purified dehydrin is highly resistant to pepsin digestion.
- Taxon
- Fagopyrum esculentumFagopyrum esculentume1
- Treatment
- pepsin digestione4
- Outcome
- highly resistant to pepsin digestione4
- Value
- 16-kDae4
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e1“dehydrin protein was purified from a Japanese variety of buckwheat seed (Fagopyrum esculentum cv.Kitawase)”
e4“a 16-kDa polypeptide that is highly resistant to pepsin digestion was produced”