Abstract
A collection of 17 monoclonal antibodies elicited against the light-harvesting chlorophyll a/b protein complex which serves photosystem II (LHC-II) of Pisum sativum shows six classes of binding specificity. Antibodies of two of the classes recognize a single polypeptide (the 28- or the 26- kD polypeptides), thereby suggesting that the two proteins are not derived from a common precursor. Other classes of antibodies cross-react with several polypeptides of LHC-II or with polypeptides of both LHC-II and the light-harvesting chlorophyll a/b polypeptides of photosystem I (LHC-I), indicating that there are structural similarities among the polypeptides of LHC-II and LHC-I. The evidence for protein processing by which the 26-, 25.5-, and 24.5-kD polypeptides are derived from a common precursor polypeptide is discussed. Binding studies using antibodies specific for individual LHC-II polypeptides were used to quantify the number of antigenic polypeptides in the thylakoid membrane. 27 copies of the 26-kD polypeptide and two copies of the 28-kD polypeptide were found per 400 chlorophylls. In the chlorina f2 mutant of barley, and in intermittent light-treated barley seedlings, the amount of the 26-kD polypeptide in the thylakoid membranes was greatly reduced, while the amount of 28-kD polypeptide was apparently not affected. We propose that stable insertion and assembly of the 28-kD polypeptide, unlike the 26-kD polypeptide, is not regulated by the presence of chlorophyll b.
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Claims 9
Claim · model-written summary
Seventeen antibodies to pea LHC-II fell into six binding-specificity classes.
- Taxon
- Pisum sativum
Lathyrus oleraceuse0 - Gene
- light-harvesting chlorophyll a/b protein complexe0
- Outcome
- six classes of binding specificitye0
- Value
- six classese0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“A collection of 17 monoclonal antibodies elicited against the light-harvesting chlorophyll a/b protein complex which serves photosystem II (LHC-II) of Pisum sativum shows six classes of binding specificity.”
Claim · model-written summary
Two antibody classes each recognized a single LHC-II polypeptide, suggesting distinct precursors.
- Taxon
- Pisum sativumLathyrus oleraceust1
- Gene
- 28- or the 26- kD polypeptidese0
- Outcome
- not derived from a common precursore0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Antibodies of two of the classes recognize a single polypeptide (the 28- or the 26- kD polypeptides), thereby suggesting that the two proteins are not derived from a common precursor.”
t0“light-harvesting chlorophyll a/b protein complex”
t1“Pisum sativum”
Claim · model-written summary
Other antibody classes cross-reacted with several LHC-II polypeptides or with LHC-I, indicating structural similarity.
- Taxon
- Pisum sativumLathyrus oleraceust1
- Gene
- LHC-IIe0
- Outcome
- cross-react with several polypeptides of LHC-IIe0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Other classes of antibodies cross-react with several polypeptides of LHC-II or with polypeptides of both LHC-II and the light-harvesting chlorophyll a/b polypeptides of photosystem I (LHC-I), indicating that there are structural similarities among the polypeptides of LHC-II and LHC-I.”
t1“Pisum sativum”
Claim · model-written summary
Pea thylakoid membranes had 27 copies of the 26-kD polypeptide per 400 chlorophylls.
- Taxon
- Pisum sativumLathyrus oleraceust1
- Gene
- 26-kD polypeptidee0
- Outcome
- 26-kD polypeptidee0
- Value
- 27 copiese0
- Qualifier
- per 400 chlorophyllse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“27 copies of the 26-kD polypeptide and two copies of the 28-kD polypeptide were found per 400 chlorophylls.”
t1“Pisum sativum”
Claim · model-written summary
Pea thylakoid membranes had two copies of the 28-kD polypeptide per 400 chlorophylls.
- Taxon
- Pisum sativumLathyrus oleraceust1
- Gene
- 28-kD polypeptidee0
- Outcome
- 28-kD polypeptidee0
- Value
- two copiese0
- Qualifier
- per 400 chlorophyllse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“27 copies of the 26-kD polypeptide and two copies of the 28-kD polypeptide were found per 400 chlorophylls.”
t1“Pisum sativum”
Claim · model-written summary
The 26-kD polypeptide was greatly reduced in chlorina f2 barley.
- Taxon
- barley
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Hordeum vulgaree0 - Material
- chlorina f2 mutante0
- Gene
- 26-kD polypeptidee0
- Outcome
- amount of the 26-kD polypeptidee0
- Direction
- greatly reducede0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
.jpg?width=500)
Verbatim
e0“In the chlorina f2 mutant of barley, and in intermittent light-treated barley seedlings, the amount of the 26-kD polypeptide in the thylakoid membranes was greatly reduced, while the amount of 28-kD polypeptide was apparently not affected.”
Claim · model-written summary
The 26-kD polypeptide was greatly reduced in barley seedlings given intermittent light.
- Taxon
- barleyHordeum vulgaree0
- Treatment
- intermittent light-treatede0
- Gene
- 26-kD polypeptidee0
- Outcome
- amount of the 26-kD polypeptidee0
- Direction
- greatly reducede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“In the chlorina f2 mutant of barley, and in intermittent light-treated barley seedlings, the amount of the 26-kD polypeptide in the thylakoid membranes was greatly reduced, while the amount of 28-kD polypeptide was apparently not affected.”
Claim · model-written summary
The 28-kD polypeptide was apparently unaffected in the tested barley conditions.
- Taxon
- barleyHordeum vulgaree0
- Gene
- 28-kD polypeptidee0
- Outcome
- amount of 28-kD polypeptidee0
- Direction
- not affectede0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“In the chlorina f2 mutant of barley, and in intermittent light-treated barley seedlings, the amount of the 26-kD polypeptide in the thylakoid membranes was greatly reduced, while the amount of 28-kD polypeptide was apparently not affected.”
Claim · model-written summary
The authors propose that stable insertion of the 28-kD polypeptide is independent of chlorophyll b.
- Taxon
- barleyHordeum vulgaree1
- Gene
- 28-kD polypeptidee0
- Compound
- chlorophyll be0
- Outcome
- stable insertion and assembly of the 28-kD polypeptidee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“We propose that stable insertion and assembly of the 28-kD polypeptide, unlike the 26-kD polypeptide, is not regulated by the presence of chlorophyll b.”
e1“chlorina f2 mutant of barley”
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See all 30 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.