Document Detail

Catalytic activation of transfer ribonucleic acid by a mammalian protein.
MedLine Citation:
PMID:  963009     Owner:  NLM     Status:  MEDLINE    
A tRNA activator has been isolated from mammalian organs which increases the capability of tRNA to accept certain amino acids through the action of mammalian aminoacyl-tRNA synthetases. This activity may be separated from the aminoacyl-tRNA synthetases for isoleucine, lysine, serine, and methionine by fractionation of liver or pancreas cytosol with ammonium sulfate or by chromatography over Sephadex G-200. The tRNA activating material is nondialyzable and is destroyed by trypsin or short heating. It acts catalytically. A molecular weight of approximately 45,000 was obtained by chromatography of tRNA activator on a calibrated Sephadex G-150 column. Activator increases acceptance of yeast tRNA for the amino acids isoleucine, leucine, lysine, serine, and methionine. It shows higher activity on liver tRNAMet f, tRNAMet m, and tRNALys than on unfractionated liver tRNA. Removal of protein from mammalian tRNA by extra phenol extractions, chromatography, or proteinase treatment increases its response to activator.
S R Dickman; D J Boll
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  15     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1976 Sep 
Date Detail:
Created Date:  1976-12-01     Completed Date:  1976-12-01     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3925-32     Citation Subset:  IM    
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MeSH Terms
Amino Acids
Cytosol / physiology
Enzyme Activation
Liver / physiology
Methionine-tRNA Ligase / metabolism
Molecular Weight
Pancreas / physiology
Proteins / isolation & purification,  pharmacology,  physiology*
RNA, Transfer / metabolism*
Transfer RNA Aminoacylation*
Reg. No./Substance:
0/Amino Acids; 0/Proteins; 9014-25-9/RNA, Transfer; EC Ligase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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