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Purification and properties of a high-molecular-mass complex between Val-tRNA synthetase and the heavy form of elongation factor 1 from mammalian cells.
The results strongly suggest that the complex of Val-tRNA synthetase withEF-1H is a novel functionally active individual form of EF-1, which is 10 times more active in the poly(U)-directed binding of Phe-tRNAPhe to ribosomes than EF- 1H. Expand
Mammalian valyl‐tRNA synthetase forms a complex with the first elongation factor
The high‐molecular‐mass form of valyl‐tRNA synthetase is associated with the first elongation factor activity and is suggested to be a novel form of the first lengthening factor. Expand
High-performance ion-exchange chromatography of oligoribonucleotides using linear and hyperbolic salt gradients.
A method for separation and chain length determination of oligo- and polynucleotides by high-performance anion-exchange chromatography was developed, which allows resolution of individual fragmentsExpand
Purification of valyl‐tRNA synthetase high‐molecular‐mass complex from rabbit liver
A high‐molecular‐mass complex containing valyl‐tRNA synthetase has been purified to homogeneity from rabbit liver and contains four polypeptides of 130, 50, 40 and 30 kDa. Expand