Claim · model-written summary
Putrescine and cadaverine had no effect on pea kinase activity.
- Taxon
- pea
Lathyrus oleraceust0 - Treatment
- putrescine and cadaverinee2
- Outcome
- kinase activitye1
- Direction
- no effecte2
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Pea Cytoplasm”
e1“The kinase activity was stimulated”
e2“putrescine and cadaverine had no effect”
Title
S. Zhang; C. D. Jin; S. J. Roux PLANT PHYSIOLOGY 1993. doi:10.1104/pp.103.3.955
Other claims from this paper (16)
- Observation A casein kinase II-type protein kinase was purified from etiolated pea plumules to about 90% purity.
- Observation The pea kinase has a tetrameric structure of two catalytic and two regulatory subunits.
- Observation The native molecular mass of the pea kinase is 150 kD.
- Observation The two catalytic subunits of the kinase have molecular masses of 41 and 40 kD.
- Observation The putative regulatory subunit of the kinase has a molecular mass of 35 kD.
- Observation Casein and phosvitin can be used as artificial substrates for the pea kinase.
- Observation Both serine and threonine residues were phosphorylated when mixed casein, beta-casein or phosvitin were the substrate.
- Observation Only serine was phosphorylated when alpha-casein or histone III-S was the substrate.
- Intervention effect Pea kinase activity was stimulated 130% by 0.5 mM spermine.
- Intervention effect Pea kinase activity was stimulated 80% by 2.5 mM spermidine.
- Intervention effect The pea kinase was very sensitive to inhibition by heparin, with an I50 of 0.025 ug/mL.
- Intervention effect The pea kinase preparation was inhibited by K+ with an I50 of 75 mM.
- Intervention effect The pea kinase preparation was inhibited by Na+ with an I50 of 65 mM.
- Intervention effect Pretreatment of the purified pea kinase with alkaline phosphatase caused a 5-fold decrease in its activity.
- Intervention effect The pea kinase lost its activity when its beta subunit was autophosphorylated in the absence of substrate.
- Mechanism The authors suggest that the activity of the casein kinase II protein kinase may be regulated by the phosphorylation state of two different sites in its multimeric structure.