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PMID: 786844 Published · ppublish English Journal Article

Multiple forms of lysyl-tRNA synthetase from Escherichia coli.

Hoppe-Seyler's Zeitschrift fur physiologische Chemie ·Vol. 357 ·No. 4 ·1976-04-00 ·Pages 543-51

Dittgen RM, Leberman R

Abstract

Lysyl-tRNA synthetase has been isolated from E. coli. The enzymatic activity elutes as three or four bands from a hydroxyl-apatite column. Polyacrylamide gel analysis shows that each of these bands contain more than one enzymatically active protein species. The molecular weights of the subunits of these species provides an explanation for the variation in the molecular weights previously reported for this enzyme.

MeSH Terms
Amino Acyl-tRNA Synthetases/isolation & purification Escherichia coli/enzymology Isoenzymes/isolation & purification Lysine-tRNA Ligase/isolation & purification Molecular Weight
Chemicals
Isoenzymes Amino Acyl-tRNA Synthetases Lysine-tRNA Ligase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Dittgen R M
Leberman R
Article Info
Journal
Hoppe-Seyler's Zeitschrift fur physiologische Chemie
Abbr.
Hoppe Seylers Z Physiol Chem
ISSN
0018-4888
Published
1976-04-00
Pages
543-51
Language
English
Region
Germany
NLM ID
2985060R
Subset
IM
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