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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1986-6-19
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pubmed:abstractText |
Two monoclonal antibodies against different epitopes in Escherichia coli ribosomal protein L7/L12 were prepared and characterized as reported previously (Sommer, A., Etchison, J.R., Gavino, G., Zecherle, N., Casiano, C., and Traud, R.R. (1985) J. Biol. Chem. 260, 6522-6527). Both antibodies strongly inhibited polyuridylic acid-directed polyphenylalanine synthesis, ribosome-dependent GTPase activity, and the binding of elongation factor G to the ribosome at mole ratios over ribosomes of 4:1 or less. One epitope was shown to be within residues 1-73 (Ab 1-73) and the other within 74-120 (Ab 74-120). Incubation of 50 S ribosomal subunits or 70 S ribosomes with Ab 1-73, but not with Ab 74-120, leads to a partial loss of L7/L12 from the particle with no loss of any other protein. The experiment was repeated with ribosomes reconstituted with pure radioactive L7/L12 of determined specific activity in order to quantify the L7/L12 in the antibody-treated particle. The protein-deficient core particles isolated by sucrose gradient centrifugation after incubation with Ab 1-73 were found to contain, on average, two copies of L7/L12 and one Ab 1-73. The constancy of this stoichiometry in many experiments and the demonstration of Ab 1-73 on all particles indicate the presence of a homogeneous population of ribosomes, each with only one of the two L7/L12 dimers originally present. The results show a difference in the interactions of the two dimers with the ribosome and present a means of preparing ribosomes with one dimer in a specific binding site. The accompanying paper (Olson, H.M., Sommer, A., Tewari, D. S., Traut, R.R., and Glitz, D.G. (1986) J. Biol. Chem. 261, 6924-6932) shows by immune electron microscopy the location of the two antibody-binding sites and the effect of Ab 1-73 on structure.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigen-Antibody Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein L7-L12
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
261
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6919-23
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2422172-Antibodies, Monoclonal,
pubmed-meshheading:2422172-Antigen-Antibody Complex,
pubmed-meshheading:2422172-Bacterial Proteins,
pubmed-meshheading:2422172-Epitopes,
pubmed-meshheading:2422172-Escherichia coli,
pubmed-meshheading:2422172-Kinetics,
pubmed-meshheading:2422172-Macromolecular Substances,
pubmed-meshheading:2422172-Ribosomal Proteins,
pubmed-meshheading:2422172-Ribosomes,
pubmed-meshheading:2422172-Sulfur Radioisotopes
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pubmed:year |
1986
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pubmed:articleTitle |
The selective release of one of the two L7/L12 dimers from the Escherichia coli ribosome induced by a monoclonal antibody to the NH2-terminal region.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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