Claim · model-written summary
The wheat leaf phosphatase had a Km of 6.554 mmol/L for pNPP hydrolysis.
Triticum aestivumNot reportedMaterialCompoundInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“in the leaves of wheat”
e0“The experiment results showed that in the dydrolysis of pNPP by phosphatase,K_m was 6.554 mmol/L and V_(max) was 0.774×10~3 U/(mg protein)”
Title
Biochemical properties of phosphatase in the leaves of wheat
Fei Meijuan; Chen Jian-sheng; Xiaoyun Wang Xibei zhiwu xuebao 2006
Other claims from this paper (12)
- Observation Vmax of the wheat leaf phosphatase in the pNPP hydrolysis was 0.774×10~3 U/(mg protein).
- Observation The optimal pH of the wheat leaf phosphatase was 6.8.
- Observation The optimal temperature of the wheat leaf phosphatase was 45℃ in a ten-minute thermal preservation.
- Observation The wheat leaf phosphatase lost 50% of its activity in 12 minutes of thermal preservation at 50 ℃.
- Observation The wheat leaf phosphatase lost 50% of its activity in 3.75 minutes of thermal preservation at 60℃.
- Observation The wheat leaf phosphatase lost 50% of its activity in 1.8 minutes of thermal preservation at 70℃.
- Intervention effect Mg2+ and Ca2+ were capable of activating the wheat leaf phosphatase.
- Intervention effect Zn2+, Cu2+ and Mn2+ inhibited the wheat leaf phosphatase activity.
- Intervention effect EDTA, sodium dihydrogen phosphate and ammonium metavanadate inhibited the wheat leaf phosphatase activity.
- Observation The non-competitive inhibition constant of the wheat leaf phosphatase was 5.87 mmol/L.
- Observation The competitive inhibition constant of the wheat leaf phosphatase was 2.47 mmol/L.
- Observation The inhibition constant of the wheat leaf phosphatase for other inhibition types was 8.2 mmol/L.