Claim · model-written summary
Humic acids did not affect inhibition of pea sinapin hydrolysis and synthesis by chlorocholine chloride, alar and hexamine.
- Taxon
- pea
Lathyrus oleraceuse1 - Treatment
- Humic acidse0
- Outcome
- inhibition of the hydrolysis and the synthesis of sinapin with chlorocholine chloride, alar and hexaminee0
- Direction
- do not affecte0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Humic acids do not affect the inhibition of choline esterase with physostigmine or the inhibition of the hydrolysis and the synthesis of sinapin with chlorocholine chloride, alar and hexamine either.”
e1“choline esterase of pea”
Title
Rita Malini de Almeida; F. Pospíšil; Květa Vacková; et al. Biologia Plantarum 1980. doi:10.1007/bf02892734
Other claims from this paper (11)
- Intervention effect Humic acids up to 100 μg ml-1 weakly affected pea choline esterase activity during sinapin hydrolysis.
- Intervention effect Higher humic acid concentrations inhibited pea choline esterase more strongly.
- Intervention effect Humic acids similarly inhibited pea choline acyltransferase-catalysed sinapin synthesis.
- Intervention effect Malathion strongly inhibited pea sinapin hydrolysis and synthesis.
- Intervention effect Malathion at 3.5 × 10-5 M inhibited pea choline esterase by 85%.
- Intervention effect Adding humic acids reduced malathion inhibition of pea choline esterase to about 8%.
- Intervention effect Humic acids prevented malathion inhibition of sinapin hydrolysis and synthesis even at low concentrations.
- Intervention effect Humic acids did not affect physostigmine inhibition of pea choline esterase.
- Intervention effect Humic acids did not affect activation of pea sinapin processes by K+ ions.
- Mechanism Humic acids were characterized as competitive inhibitors of pea choline esterase.
- Mechanism Malathion inhibition of pea choline esterase was characterized as acompetitive to noncompetitive.