Claim · model-written summary
Alfalfa beta-amylase had isoelectric point 4.8.
- Taxon
- alfalfa
Medicago sativae0 - Gene
- beta-amylasee0
- Outcome
- isoelectric pointe0
- Value
- 4.8e0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The optimum pH and isoelectric point of alfalfa beta-amylase were 7.0 and 4.8, respectively, which were different from other plant beta-amylases.”
Title
Purification of β-Amylase from Alfalfa (Medicago sativa L.) Seeds
Akiko Kohno; Takashi Nanmori; Ryu Shinke The Journal of Biochemistry 1989. doi:10.1093/oxfordjournals.jbchem.a122644
Other claims from this paper (6)
- Method / resource Chromatofocusing separated alfalfa amylase to a homogeneous state.
- Observation Purified alfalfa amylase was identified as beta-amylase because soluble starch degradation formed only beta-maltose.
- Observation Alfalfa beta-amylase had molecular weight 61,000.
- Observation Alfalfa beta-amylase had specific activity 1,077 A.U./mg.
- Intervention effect Modification of sulfhydryl groups with p-chloromercuribenzoic acid inhibited alfalfa beta-amylase activity.
- Observation Alfalfa beta-amylase had optimum pH 7.0.