Paper · 1990 · Physiologia Plantarum

Peroxidase‐mediated chlorophyll bleaching in degreening canola (Brassica napus) seeds and its inhibition by sublethal freezing

A. M. Johnson‐Flanagan; G. McLachlan

8
claims
15
verbatim quotes
26
citations
1
research areas
—
Not open access

Abstract

Peroxidase activity in isolated thylakoids from degreening canola ( Brassica napus cv. Westar) seeds was demonstrated. The enzyme catalyzes the degradation of thylakoid‐bound pigments in the presence of H 2 O 2 and 2,4‐dichlorophenol. Peroxidase activity is related to degreening, with periods of rapid degreening associated with high enzyme activity. Both de novo synthesis and substrate availability appear to control enzyme activity. Peroxidase is initially inhibited and then stimulated by sublethal freezing. Therefore, inhibition of peroxidase activity following sublethal freezing may be responsible, in part, for a failure of the seed to degreen.

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Claims 8

Observationobservedoriginal resultmeasured

Claim · model-written summary

Peroxidase activity was demonstrated in thylakoids from degreening canola seeds.

Material
Westare0
Organ / stage
seedse0
Gene
Peroxidasee0
Outcome
Peroxidase activitye0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Brassica napus var. napus
Brassica napus var. napus · Taxoncontri from Yonezawa-Shi, Yamagata, Japan · CC BY-SA 2.0 · Wikimedia Commons ↗

Verbatim

e0

“Peroxidase activity in isolated thylakoids from degreening canola ( Brassica napus cv. Westar) seeds was demonstrated”

✓ located verbatim in the source · abstract, characters 0–117 · show in text ↑
Mechanismauthor interpretationoriginal resultmeasured

Claim · model-written summary

Peroxidase catalyzes degradation of thylakoid pigments in the presence of hydrogen peroxide and 2,4-dichlorophenol.

Gene
enzymee0
Compound
H 2 O 2 and 2,4‐dichlorophenole0
Outcome
degradation of thylakoid‐bound pigmentse0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Brassica napus var. napus
Brassica napus var. napus · Taxoncontri from Yonezawa-Shi, Yamagata, Japan · CC BY-SA 2.0 · Wikimedia Commons ↗

Verbatim

e0

“The enzyme catalyzes the degradation of thylakoid‐bound pigments in the presence of H 2 O 2 and 2,4‐dichlorophenol”

✓ located verbatim in the source · abstract, characters 119–233 · show in text ↑
t0

“canola”

✓ located verbatim in the source · title, characters 56–62 · show in text ↑
Associationobservedoriginal resultmeasured

Claim · model-written summary

Rapid seed degreening is associated with high peroxidase activity.

Gene
enzyme activitye0
Outcome
rapid degreeninge0

Not reportedDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Brassica napus var. napus
Brassica napus var. napus · Taxoncontri from Yonezawa-Shi, Yamagata, Japan · CC BY-SA 2.0 · Wikimedia Commons ↗

Verbatim

e0

“periods of rapid degreening associated with high enzyme activity”

✓ located verbatim in the source · abstract, characters 286–350 · show in text ↑
t0

“canola”

✓ located verbatim in the source · title, characters 56–62 · show in text ↑
Mechanismauthor interpretationoriginal resultmeasured

Claim · model-written summary

De novo synthesis appears to control peroxidase activity.

Outcome
enzyme activitye0
Qualifier
de novo synthesise0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Brassica napus var. napus
Brassica napus var. napus · Taxoncontri from Yonezawa-Shi, Yamagata, Japan · CC BY-SA 2.0 · Wikimedia Commons ↗

Verbatim

e0

“Both de novo synthesis and substrate availability appear to control enzyme activity”

✓ located verbatim in the source · abstract, characters 352–435 · show in text ↑
t0

“canola”

✓ located verbatim in the source · title, characters 56–62 · show in text ↑
Mechanismauthor interpretationoriginal resultmeasured

Claim · model-written summary

Substrate availability appears to control peroxidase activity.

Outcome
enzyme activitye0
Qualifier
substrate availabilitye0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Brassica napus var. napus
Brassica napus var. napus · Taxoncontri from Yonezawa-Shi, Yamagata, Japan · CC BY-SA 2.0 · Wikimedia Commons ↗

Verbatim

e0

“Both de novo synthesis and substrate availability appear to control enzyme activity”

✓ located verbatim in the source · abstract, characters 352–435 · show in text ↑
t0

“canola”

✓ located verbatim in the source · title, characters 56–62 · show in text ↑
Intervention effectobservedoriginal resultnegativemeasured

Claim · model-written summary

Sublethal freezing initially inhibits peroxidase activity.

Treatment
sublethal freezinge0
Outcome
Peroxidasee0
Direction
inhibitede0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Brassica napus var. napus
Brassica napus var. napus · Taxoncontri from Yonezawa-Shi, Yamagata, Japan · CC BY-SA 2.0 · Wikimedia Commons ↗

Verbatim

e0

“Peroxidase is initially inhibited and then stimulated by sublethal freezing”

✓ located verbatim in the source · abstract, characters 437–512 · show in text ↑
t0

“canola”

✓ located verbatim in the source · title, characters 56–62 · show in text ↑
Intervention effectobservedoriginal resultpositivemeasured

Claim · model-written summary

Sublethal freezing subsequently stimulates peroxidase activity.

Treatment
sublethal freezinge0
Outcome
Peroxidasee0
Direction
stimulatede0

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Brassica napus var. napus
Brassica napus var. napus · Taxoncontri from Yonezawa-Shi, Yamagata, Japan · CC BY-SA 2.0 · Wikimedia Commons ↗

Verbatim

e0

“Peroxidase is initially inhibited and then stimulated by sublethal freezing”

✓ located verbatim in the source · abstract, characters 437–512 · show in text ↑
t0

“canola”

✓ located verbatim in the source · title, characters 56–62 · show in text ↑
Mechanismhypothesisoriginal resultnegativemeasured

Claim · model-written summary

Freezing-related inhibition of peroxidase may partly cause failure of seeds to degreen.

Treatment
sublethal freezinge0
Outcome
failure of the seed to degreene0
Qualifier
may be responsible, in parte0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Brassica napus var. napus
Brassica napus var. napus · Taxoncontri from Yonezawa-Shi, Yamagata, Japan · CC BY-SA 2.0 · Wikimedia Commons ↗

Verbatim

e0

“inhibition of peroxidase activity following sublethal freezing may be responsible, in part, for a failure of the seed to degreen”

✓ located verbatim in the source · abstract, characters 525–653 · show in text ↑
t0

“canola”

✓ located verbatim in the source · title, characters 56–62 · show in text ↑

cold · physiology: antioxidant enzymes · Brassica napus (oilseed rape)Results agree

5 papers: 5 positive, 0 negative or no effect

4 papers in the same direction as this paper

  1. positive
  2. positive
  3. positive

1 paper more in this group

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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.