Claim · model-written summary
had both peroxidase and catalase activities
- Outcome
- peroxidase and catalase activitiese0
SorghumNot reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“had both peroxidase and catalase activities”
t0“Sorghum”
Title
A Monophenol Oxidase Activity in Extracts of Sorghum
H. A. Stafford; R. Baldy PLANT PHYSIOLOGY 1970. doi:10.1104/pp.45.2.215
Other claims from this paper (12)
- Observation A p-hydroxycinnamic acid oxidase activity was present in enzyme preparations from first internodes of Sorghum vulgare variety Wheatland milo when incubated in phosphate buffer at pH 7.5
- Observation This preparation had no classical polyphenolase activity
- Observation A second substrate was p-hydroxyphenylpyruvic acid
- Observation Ferulic acid was slightly active at low concentrations and inhibitory at higher ones
- Observation Diphenols such as caffeic and chlorogenic acids were inactive and inhibitory to p-hydroxycinnamic acid oxidation
- Observation A variety of monophenols such as tyrosine and cinnamic acid were inactive
- Observation A sulfhydryl reducing agent at the 5 millimolar level such as mercaptoethanol, reduced glutathione, or dithiothreitol was obligatory
- Observation about 1 micromole of O(2) was consumed per micromole of p-hydroxycinnamic acid that disappeared in the presence of mercaptoethanol
- Observation about 2 micromoles of O(2) were consumed per micromole of p-hydroxycinnamic acid that disappeared
- Observation Potassium cyanide, diethyldithiocarbamate, ascorbic acid, and ethylenediaminetetraacetate were inhibitory
- Observation The activity was present in both soluble and particulate (500 to 100,000 gravity) fractions of internodes
- Observation The ratelimiting step was the hydroxylation of p-hydroxycinnamic acid