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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1991-5-23
|
| pubmed:abstractText |
A 7.5-kDa protein has been isolated from chlorosomes of Chlorobium limicola f. thiosulfatophilum and the complete primary structure determined by a combination of automatic Edman degradation and plasma desorption mass spectrometry. The 74-residue protein shows great homology to a similar protein of unknown function which has been isolated from Pelodictyon luteolum but otherwise no significant homology to other proteins can be found. The possible role of the protein in the structure and function of the chlorosome is discussed.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
8
|
| pubmed:volume |
1077
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
220-4
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2015294-Amino Acid Sequence,
pubmed-meshheading:2015294-Chromatography, High Pressure Liquid,
pubmed-meshheading:2015294-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2015294-Eubacterium,
pubmed-meshheading:2015294-Hydrolysis,
pubmed-meshheading:2015294-Mass Spectrometry,
pubmed-meshheading:2015294-Molecular Sequence Data,
pubmed-meshheading:2015294-Molecular Weight,
pubmed-meshheading:2015294-Photosynthetic Reaction Center Complex Proteins
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
The amino acid sequence of a major protein component in the light harvesting complex of the green photosynthetic bacterium Chlorobium limicola f. thiosulfatophilum.
|
| pubmed:affiliation |
Department of Molecular Biology, Odense University, Denmark.
|
| pubmed:publicationType |
Journal Article
|