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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1972-11-18
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pubmed:abstractText |
1. Transferase I of rat liver binds aminoacyl-tRNA to form a relatively stable complex, which is retained on cellulose nitrate filters. This reaction proceeds at both 0 degrees C and 37 degrees C and is inhibited by GTP. The resulting product is stabilized by GTP and Mg(2+). 2. Only very low quantities of deacylated tRNA are bound by transferase I. 3. Methods are described for the preparative isolation of the transferase I-aminoacyl-tRNA complex from incubation mixtures by using ion-exchange procedures. 4. The transferase I-aminoacyl-tRNA complex becomes readily bound to ribosomes. The presence of Mg(2+) is essential for the binding. GTP stimulates this reaction but is not absolutely required. 5. It is concluded that the formation of the transferase I-aminoacyl-tRNA complex may be the primary reaction in the binding of aminoacyl-tRNA to mammalian ribosomes and that, unlike in bacterial systems, GTP is not absolutely required for this step.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4289971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4308855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4314911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4318853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4867665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4868218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4878450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4897025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4897244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-4908538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-5073244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-5124397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-5248824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-5479828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-5638595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5073243-6073038
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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 |
Feb
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
126
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
923-31
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:5073243-Amino Acids,
pubmed-meshheading:5073243-Animals,
pubmed-meshheading:5073243-Chromatography, Gel,
pubmed-meshheading:5073243-Female,
pubmed-meshheading:5073243-Guanosine Triphosphate,
pubmed-meshheading:5073243-Liver,
pubmed-meshheading:5073243-Magnesium,
pubmed-meshheading:5073243-Male,
pubmed-meshheading:5073243-Phosphorus Isotopes,
pubmed-meshheading:5073243-Protein Binding,
pubmed-meshheading:5073243-RNA, Transfer,
pubmed-meshheading:5073243-Rats,
pubmed-meshheading:5073243-Ribosomes,
pubmed-meshheading:5073243-Transferases
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pubmed:year |
1972
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pubmed:articleTitle |
Intermediate reactions in the binding of aminoacyl-transfer ribonucleic acid to rat liver ribosomes. Formation and properties of an aminoacyl-transfer ribonucleic acid-transferase I complex.
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pubmed:publicationType |
Journal Article,
In Vitro
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