Claim · model-written summary
The animal-cell phosphatase identification and quantification procedure was applicable to higher plants.
- Taxon
- higher plantsEmbryophytae0
- Outcome
- is applicable to higher plantse0
- Comparator
- animal cellse0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentSettingDirectionValueQualifier
Verbatim
e0“the improved procedure for identifying and quantifying protein phosphatases in animal cells is applicable to higher plants”
Title
Identification of high levels of type 1 and type 2A protein phosphatases in higher plants
C MacKintosh; P Cohen Biochemical Journal 1989. doi:10.1042/bj2620335
Other claims from this paper (13)
- Observation Oilseed rape seeds contain type 1 and type 2A phosphatases with properties indistinguishable from mammalian counterparts.
- Observation Plant type 1 activity selectively dephosphorylated the beta-subunit of phosphorylase kinase.
- Intervention effect Okadaic acid inhibited type 1 activity with an approximate IC50 of 10 nM.
- Intervention effect Mammalian inhibitor 1 inhibited plant type 1 activity with IC50 0.6 nM.
- Intervention effect Mammalian inhibitor 2 inhibited plant type 1 activity with IC50 2.0 nM.
- Observation Plant type 2A preferentially dephosphorylated the alpha-subunit of phosphorylase kinase.
- Intervention effect Plant type 2A was sensitive to okadaic acid at approximately 0.1 nM IC50.
- Intervention effect Inhibitors 1 and 2 did not affect plant type 2A activity.
- Observation Forty percent of plant type 1 activity was particulate.
- Observation Plant type 2A phosphatase was cytosolic.
- Observation Plant type 1 and 2A specific activities were as high as in mammalian extracts.
- Observation No type 2B or type 2C activity was detected.
- Method / resource The authors suggest okadaic acid may identify plant enzymes regulated by reversible phosphorylation.