Biopolym. Cell. 1991; 7(6):83-88.
Structure and Function of Biopolymers
Properties of tryptophan fluorescence of two forms of tyrosyl-tRNA synthetase from bovine liver
1Klimenko I. V., 1Guscha T. O., 1Kornelyuk A. I.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680


The properties of intrinsic tryptophan fluorescence of two forms (molecular weight 2X 59 000 and 2X39 000) of tyrosyl-tRNA synthetase from bovine liver have been studied. The contributions of exposed and internal tryptophan residues into fluorescence spectrum of tyrosyl-tRNA synthetase have been determined in terms of the model of discrete structure-physical classes of tryptophanyls in the proteins. The temperature dependence of parameters of tryptophan fluorescence testified that temperature-induced mobility of separate protein fragments increased in temperature range from 40 °C to 75 °C. Analysis of temperature quenching of enzyme fluorescence in co-ordinate of the 1/q(T) and 1/q(T/η) indicated that the mobility of synthetase in the solution was regulated by diffusion characteristics of the solvent. It is true both for surface and for internal parts of protein.


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