Claim · model-written summary
Both chains contain many hydrophilic residues.
- Taxon
- Capparis masaikai Lévl.Capparis masaikaie1
- Outcome
- hydrophilic amino acid residuese0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Verbatim
e0“The A chain is mostly composed of hydrophilic amino acid residues and the B chain also contains many hydrophilic residues”
e1“from the seeds of Capparis masaikai Lévl.”
Title
Xiaozhu LIU; Shoji MAEDA; Zhong HU; et al. European Journal of Biochemistry 1993. doi:10.1111/j.1432-1033.1993.tb19896.x
Other claims from this paper (9)
- Observation Mabinlin II sweetness was unchanged after prolonged near-boiling incubation.
- Observation Purified mabinlin II appeared as a 14 kDa band.
- Observation With dithiothreitol, mabinlin II produced a 4.6 kDa band.
- Observation With dithiothreitol, mabinlin II produced a 5.2 kDa band.
- Observation The reduced protein yielded separate A and B chains.
- Method / resource The amino acid sequences of both chains were determined.
- Observation The A chain has 33 amino acid residues.
- Observation The B chain has 72 amino acid residues.
- Association Mabinlin II sequence was highly similar to 2S seed storage proteins, especially Arabidopsis AT2S3.