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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1990-6-21
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pubmed:abstractText |
C-factor, a Myxococcus xanthus protein that restores the developmental defects of a class of nonautonomous mutants resulting from mutation of the csgA gene, has been purified approximately 1000-fold from starved wild-type cells. The monomeric form of C-factor is a single polypeptide with a molecular mass of 17 kDa that can be solubilized by detergent from membrane components. Characterization by gel filtration and denaturing gel electrophoresis suggests that biologically active C-factor is a dimer composed of two 17-kDa monomers. Antibodies against a form of the M. xanthus csgA gene product overexpressed in Escherichia coli react with purified C-factor.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-16593290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-2152896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-2828174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-2830469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-3017794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-3523128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-3932110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-4029507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-6091110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-6162199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-6402495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-6806248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-6811561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-806967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2111012-98366
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3635-9
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:2111012-Bacterial Proteins,
pubmed-meshheading:2111012-Cholic Acids,
pubmed-meshheading:2111012-Chromatography, Gel,
pubmed-meshheading:2111012-Chromatography, Ion Exchange,
pubmed-meshheading:2111012-Genes, Bacterial,
pubmed-meshheading:2111012-Kinetics,
pubmed-meshheading:2111012-Molecular Weight,
pubmed-meshheading:2111012-Mutation,
pubmed-meshheading:2111012-Myxococcales,
pubmed-meshheading:2111012-Solubility,
pubmed-meshheading:2111012-Spores, Bacterial,
pubmed-meshheading:2111012-Ultrafiltration
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pubmed:year |
1990
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pubmed:articleTitle |
Purification and properties of Myxococcus xanthus C-factor, an intercellular signaling protein.
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pubmed:affiliation |
Department of Biochemistry, Stanford University School of Medicine, California 94305.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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