Claim · model-written summary
DHAP reductase was isolated from Dunaliella in 50% yield and located in chloroplasts.
- Taxon
- Dunaliella tertiolectaDunaliella tertiolectae0
- Organ / stage
- chloroplastse0
- Gene
- dihydroxyacetone phosphate (DHAP) reductasee0
- Outcome
- 50% yielde0
Not reportedMaterialCompoundInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Verbatim
e0“A dihydroxyacetone phosphate (DHAP) reductase has been isolated in 50% yield from Dunaliella tertiolecta by rapid chromatography on diethylaminoethyl cellulose. The activity was located in the chloroplasts.”
Title
Robert Gee; Arun Goyal; Dennis Gerber; et al. PLANT PHYSIOLOGY 1988. doi:10.1104/pp.88.3.896
Other claims from this paper (7)
- Observation Spinach reductase isoforms were not activated by heat.
- Observation Leaf thioredoxin stimulated spinach chloroplast DHAP reductase.
- Observation Traces of detergents completely inhibited higher plant reductases.
- Observation Salts inhibited spinach chloroplast reductase.
- Observation Phosphate stimulated spinach chloroplast reductase.
- Observation Spinach chloroplast DHAP reductase had little NADPH activity above pH 7.0.
- Observation Spinach chloroplast enzyme appears to use NADH in vivo, while the cytosolic isozyme may use either nucleotide.