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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1982-1-9
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pubmed:abstractText |
The topography of the photosynthetic reaction center (RC) polypeptides (H, M, and L) was investigated by proteolysis and radioiodination of membrane vesicles isolated from Rhodopseudomonas sphaeroides. Chromatophores, obtained from French-pressed cell lysates, are closed vesicles' and oriented inside out with respect to the cytoplasmic membrane (cytoplasmic side out). Spheroplast-derived vesicles (SDVs), obtained after osmotic lysis of lysozyme-treated cells, are oriented right side in (periplasmic side out). Alpha-Chymotrypsin treatment of chromatophores and trypsin treatment of SDVs resulted in cleavage of H. Alpha-Chymotrypsin treatment of SDVs did not cleave H, and trypsin treatment of chromatophores did not consistently cleave this polypeptide. M and L of both vesicles were apparently not affected by these proteases. The SDV trypsin cleavage product of H was identified by alpha-chymotryptic (125)I-labeled peptide mapping and had a molecular weight of 26 000. Membrane surface radioiodination with chloroglycoluril coated on glass tubes resulted in preferential labeling of H and M of SDVs and chromatophores. The radiospecific activities of H, M, and L were higher with labeling of SDVs as compared to labeling of chromatophores. Alpha-Chymotryptic (125)I-labeled peptide maps of H, M, and L from surface-radioiodinated SDVs differed from the corresponding maps of these polypeptides from surface-radioiodinated chromatophores. The results indicate the asymmetric exposure of H, M, and L on opposite surfaces of the R. sphaeroides membrane. Exposed iodination sites of these polypeptides are more abundant on the periplasmic surface than on the cytoplasmic surface of this membrane.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4590-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7028090-Bacterial Proteins,
pubmed-meshheading:7028090-Chymotrypsin,
pubmed-meshheading:7028090-Kinetics,
pubmed-meshheading:7028090-Peptide Fragments,
pubmed-meshheading:7028090-Photosynthesis,
pubmed-meshheading:7028090-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:7028090-Protein Conformation,
pubmed-meshheading:7028090-Rhodobacter sphaeroides,
pubmed-meshheading:7028090-Trypsin
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pubmed:year |
1981
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pubmed:articleTitle |
Membrane topography of the photosynthetic reaction center polypeptides of Rhodopseudomonas sphaeroides.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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