Abstract
Indole-3-acetic acid is oxidized to oxindole-3-acetic acid by Zea mays tissue extracts. Shoot, root, and endosperm tissues have enzyme activities of 1 to 10 picomoles per hour per milligram protein. The enzyme is heat labile, is soluble, and requires oxygen for activity. Cofactors of mixed function oxygenase, peroxidase, and intermolecular dioxygenase are not stimulatory to enzymic activity. A heat-stable, detergent-extractable component from corn enhances enzyme activity 6- to 10-fold. This is the first demonstration of the in vitro enzymic oxidation of indole-3-acetic acid to oxindole-3-acetic acid in higher plants.
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Claims 5
Claim · model-written summary
Zea mays tissue extracts oxidized indole-3-acetic acid to oxindole-3-acetic acid.
- Outcome
- Indole-3-acetic acid is oxidized to oxindole-3-acetic acide0
Zea maysOrganisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Indole-3-acetic acid is oxidized to oxindole-3-acetic acid by Zea mays tissue extracts.”
Claim · model-written summary
Shoot, root, and endosperm tissue extracts had enzyme activity of 1 to 10 picomoles per hour per milligram protein.
- Organ / stage
- Shoot, root, and endosperm tissuese0
- Outcome
- enzyme activitiese0
- Value
- 1 to 10 picomoles per hour per milligram proteine0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Shoot, root, and endosperm tissues have enzyme activities of 1 to 10 picomoles per hour per milligram protein.”
t0“Zea mays”
Claim · model-written summary
The enzyme was heat labile and soluble and required oxygen for activity.
- Outcome
- heat labile, is soluble, and requires oxygen for activitye0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The enzyme is heat labile, is soluble, and requires oxygen for activity.”
t0“Zea mays”
Claim · model-written summary
The tested oxygenase, peroxidase, and dioxygenase cofactors did not stimulate enzyme activity.
- Treatment
- Cofactors of mixed function oxygenase, peroxidase, and intermolecular dioxygenasee0
- Outcome
- enzymic activitye0
- Direction
- not stimulatorye0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Cofactors of mixed function oxygenase, peroxidase, and intermolecular dioxygenase are not stimulatory to enzymic activity.”
t0“Zea mays”
Claim · model-written summary
A heat-stable, detergent-extractable corn component enhanced enzyme activity 6- to 10-fold.
- Taxon
- corn
Zea mays subsp. mayse0 - Treatment
- A heat-stable, detergent-extractable component from corne0
- Outcome
- enzyme activitye0
- Direction
- enhancese0
- Value
- 6- to 10-folde0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“A heat-stable, detergent-extractable component from corn enhances enzyme activity 6- to 10-fold.”
The same questions in other papers
Zea mays subsp. mays · soil: biology · Zea mays (maize)Positive and negative results
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- negative
- negative
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See all 9 papers →cofactor · physiology: enzyme activity · Zea mays (maize)Results agree
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- no effect
Peroxidase · physiology: enzyme activity · Zea mays (maize)Results agree
1 paper in the same direction as this paper
- no effect
heat · soil: biology · Zea mays (maize)Positive and negative results
2 papers in the same direction as this paper · 4 in the opposite direction
- negative
- negative
- negative
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See all 7 papers →Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.