Claim · model-written summary
The P phi B adduct had properties nearly indistinguishable from native photoreceptor.
- Taxon
- oat
Avena sativat0 - Outcome
- spectrophotometric propertiese0
- Direction
- nearly indistinguishablee0
- Comparator
- native photoreceptore0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the P phi B adduct displaying spectrophotometric properties nearly indistinguishable from those of the native photoreceptor”
t0“Oat”
Title
Purification and Characterization of Recombinant Affinity Peptide‐Tagged Oat Phytochrome A
John T. Murphy; J. Clark Lagarias Photochemistry and Photobiology 1997. doi:10.1111/j.1751-1097.1997.tb01920.x
Other claims from this paper (9)
- Method / resource Full-length oat phytochrome A was purified to apparent homogeneity from yeast expression.
- Observation Tagged ASPHYA yielded a 124 kDa polypeptide.
- Method / resource ASPHYA-ST bound streptavidin agarose and eluted with 45% chromatographic efficiency.
- Observation P phi B and PCB adducts were photoactive.
- Observation The PCB adduct had blue-shifted absorption maxima.
- Observation The PEB adduct was photochemically inactive but fluorescent.
- Observation PEB adduct excitation peaked at 576 nm.
- Observation PEB adduct emission peaked at 586 nm.
- Observation ASPHYA-ST and its three bilin adducts were homodimers.