Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
Mammalian valyl‐tRNA synthetase forms a complex with the first elongation factor
Purification and properties of a high-molecular-mass complex between Val-tRNA synthetase and the heavy form of elongation factor 1 from mammalian cells.
- Y. Motorin, A. Wolfson, D. Löhr, A. F. Orlovsky, K. Gladilin
- Biology, ChemistryEuropean journal of biochemistry
- 1 October 1991
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.
Crystal structures of native and recombinant yeast fumarase.
Crystal structures for both native and recombinant forms of yeast fumarase from Saccharomyces cerevisiae have been completed to moderate resolution by two separate laboratories, providing further evidence that an active-site water molecule may play an active role in the fumarases-catalyzed reaction.
Evolution of self-assembly of probionts.
Purification of valyl‐tRNA synthetase high‐molecular‐mass complex from rabbit liver
Anticodon‐dependent aminoacylation of RNA minisubstrate by lysyl‐tRNA synthetase
Purification, characterization and preliminary X-ray study of fumarase from Saccharomyces cerevisiae.
[Determination of the average dimensions and number of coacervate drops by Tyndall spectra].
DNA content of radiosensitive organs of albino rats exposed to radiation at high altitude and following adaptation to hypoxia in a pressure chamber. [Gamma radiation]
- F. T. Guseinov, I. Egorov, Komolova Gs, A. Shafirkin, B. U. Moldotashev, K. Gladilin
- Biology, Medicine
In the postradiation recovery period, the levels of DNA in the animal organs examined, after exposure to hypoxia, were higher than in the organs of the corresponding nonirradiated control animals, however, this effect depends on the distinctions of the organ and exposure to Hypoxia.
[Effect of complex formation of Escherichia coli beta-galactosidase with polyelectrolytes on its kinetic characteristics].