Abstract
Chloroplast thylakoid protein phosphatase activity was measured using (32)P-labeled histone as an exogenous substrate and an assay of the (32)Pi released involving formation of a phosphomolybdate complex and organic extraction. The activity was liberated from wheat (Triticum aestivum) thylakoids by washing the membranes in NaCl-containing solutions followed by centrifugation. The liberated phosphatase activity had a pH optimum of approximately 6.75, was inhibited by addition of 10 millimolar EDTA or EGTA, and was stimulated by addition of millimolar amounts of dithiothreitol, magnesium, manganese, or calcium ions. The rate of thylakoid protein dephosphorylation was decreased following liberation of a portion of the protein phosphatase activity and was increased by addition of salt-liberated phosphatase fraction. These results suggest that at least a portion of wheat thylakoid protein phosphatase is a peripheral, rather than an integral, membrane protein.
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Claims 11
Claim · model-written summary
NaCl washing liberated phosphatase activity from wheat thylakoids.
- Taxon
- wheat
Triticum aestivume0 - Organ / stage
- thylakoidse0
- Treatment
- washing the membranes in NaCl-containing solutionse0
- Outcome
- activity was liberatede0
Not reportedComparatorDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The activity was liberated from wheat (Triticum aestivum) thylakoids by washing the membranes in NaCl-containing solutions followed by centrifugation”
Claim · model-written summary
Liberated phosphatase activity had an approximate pH optimum of 6.75.
- Taxon
- wheatTriticum aestivumt0
- Outcome
- pH optimume0
- Value
- approximately 6.75e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The liberated phosphatase activity had a pH optimum of approximately 6.75”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
EDTA inhibited liberated phosphatase activity.
- Taxon
- wheatTriticum aestivumt0
- Treatment
- 10 millimolar EDTAe0
- Outcome
- phosphatase activitye0
- Direction
- inhibitede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The liberated phosphatase activity had a pH optimum of approximately 6.75, was inhibited by addition of 10 millimolar EDTA or EGTA”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
EGTA inhibited liberated phosphatase activity.
- Taxon
- wheatTriticum aestivumt0
- Treatment
- EGTAe0
- Outcome
- phosphatase activitye0
- Direction
- inhibitede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The liberated phosphatase activity had a pH optimum of approximately 6.75, was inhibited by addition of 10 millimolar EDTA or EGTA”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
Dithiothreitol stimulated liberated phosphatase activity.
- Taxon
- wheatTriticum aestivumt0
- Treatment
- dithiothreitole0
- Outcome
- phosphatase activitye0
- Direction
- stimulatede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The liberated phosphatase activity had a pH optimum of approximately 6.75, was inhibited by addition of 10 millimolar EDTA or EGTA, and was stimulated by addition of millimolar amounts of dithiothreitol, magnesium, manganese, or calcium ions”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
Magnesium stimulated liberated phosphatase activity.
- Taxon
- wheatTriticum aestivumt0
- Treatment
- magnesiume0
- Outcome
- phosphatase activitye0
- Direction
- stimulatede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The liberated phosphatase activity had a pH optimum of approximately 6.75, was inhibited by addition of 10 millimolar EDTA or EGTA, and was stimulated by addition of millimolar amounts of dithiothreitol, magnesium, manganese, or calcium ions”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
Manganese stimulated liberated phosphatase activity.
- Taxon
- wheatTriticum aestivumt0
- Treatment
- manganesee0
- Outcome
- phosphatase activitye0
- Direction
- stimulatede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The liberated phosphatase activity had a pH optimum of approximately 6.75, was inhibited by addition of 10 millimolar EDTA or EGTA, and was stimulated by addition of millimolar amounts of dithiothreitol, magnesium, manganese, or calcium ions”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
Calcium stimulated liberated phosphatase activity.
- Taxon
- wheatTriticum aestivumt0
- Treatment
- calcium ionse0
- Outcome
- phosphatase activitye0
- Direction
- stimulatede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The liberated phosphatase activity had a pH optimum of approximately 6.75, was inhibited by addition of 10 millimolar EDTA or EGTA, and was stimulated by addition of millimolar amounts of dithiothreitol, magnesium, manganese, or calcium ions”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
Liberating phosphatase decreased thylakoid protein dephosphorylation rate.
- Taxon
- wheatTriticum aestivumt0
- Treatment
- liberation of a portion of the protein phosphatase activitye0
- Outcome
- rate of thylakoid protein dephosphorylatione0
- Direction
- decreasede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The rate of thylakoid protein dephosphorylation was decreased following liberation of a portion of the protein phosphatase activity”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
Adding the salt-liberated phosphatase fraction increased dephosphorylation rate.
- Taxon
- wheatTriticum aestivumt0
- Treatment
- addition of salt-liberated phosphatase fractione0
- Outcome
- rate of thylakoid protein dephosphorylatione0
- Direction
- increasede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The rate of thylakoid protein dephosphorylation was decreased following liberation of a portion of the protein phosphatase activity and was increased by addition of salt-liberated phosphatase fraction”
t0“wheat (Triticum aestivum) thylakoids”
Claim · model-written summary
The authors infer that some wheat thylakoid phosphatase is a peripheral membrane protein.
- Taxon
- wheatTriticum aestivume0
- Gene
- thylakoid protein phosphatasee0
- Outcome
- peripheral, rather than an integral, membrane proteine0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“at least a portion of wheat thylakoid protein phosphatase is a peripheral, rather than an integral, membrane protein”
The same questions in other papers
manganese atom · soil: biology · Triticum aestivum (wheat)Results agree
1 paper in the same direction as this paper
- positive
magnesium atom · soil: biology · Triticum aestivum (wheat)Results agree
1 paper in the same direction as this paper
- positive
salinity · quality: protein · Triticum aestivum (wheat)Results differ
6 papers in the same direction as this paper · 12 in the opposite direction
- negative
- negative
- negative
15 papers more in this group
See all 19 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.