Abstract
The N-terminal sequence of the spinach chloroplast reductase-binding protein was determined. The sequence is the same one of a 16.5-kDa polypeptide described as a component of the oxygen-evolving system. Antibodies against both proteins are equivalent as shown by immunoblots, Ouchterlony assays, precipitation of reductase-binding protein complex, and agglutination of thylakoids partially depleted of reductase. These results suggest both proteins are identical. Exposure of the binding protein on the stromal side of thylakoids is supported by agglutination of thylakoids partially depleted of reductase, proteolysis by trypsin, and by accessibility to Fab of anti-binding protein. The latter prevents rebinding of reductase supporting the functional role of the binding protein (16.5 kDa).
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Claims 5
Claim · model-written summary
The spinach reductase-binding protein N-terminal sequence matched that of the 16.5-kDa polypeptide.
- Taxon
- spinach
Spinacia oleraceae0 - Gene
- chloroplast reductase-binding proteine0
- Outcome
- sequence is the same one of a 16.5-kDa polypeptidee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The N-terminal sequence of the spinach chloroplast reductase-binding protein was determined. The sequence is the same one of a 16.5-kDa polypeptide described as a component of the oxygen-evolving system”
Claim · model-written summary
Antibodies against the two proteins were equivalent.
- Taxon
- spinachSpinacia oleraceae1
- Outcome
- Antibodies against both proteins are equivalente0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Antibodies against both proteins are equivalent as shown by immunoblots, Ouchterlony assays, precipitation of reductase-binding protein complex, and agglutination of thylakoids partially depleted of reductase”
e1“spinach chloroplast reductase-binding protein”
Claim · model-written summary
The authors suggest the two proteins are identical.
- Taxon
- spinachSpinacia oleraceae1
- Outcome
- both proteins are identicale0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“These results suggest both proteins are identical”
e1“spinach chloroplast reductase-binding protein”
Claim · model-written summary
Experiments supported exposure of the binding protein on the stromal side of thylakoids.
- Taxon
- spinachSpinacia oleraceae1
- Gene
- binding proteine0
- Outcome
- Exposure of the binding protein on the stromal side of thylakoidse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Exposure of the binding protein on the stromal side of thylakoids is supported by agglutination of thylakoids partially depleted of reductase, proteolysis by trypsin, and by accessibility to Fab of anti-binding protein”
e1“spinach chloroplast reductase-binding protein”
Claim · model-written summary
Fab of anti-binding protein prevented reductase rebinding, supporting a functional role.
- Taxon
- spinachSpinacia oleraceae1
- Gene
- binding proteine0
- Outcome
- prevents rebinding of reductasee0
- Qualifier
- functional role of the binding proteine0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The latter prevents rebinding of reductase supporting the functional role of the binding protein (16.5 kDa)”
e1“spinach chloroplast reductase-binding protein”