Abstract
This chapter describes the isolation of tryptophanyl-tRNA synthetase [L-tryptophan: tRNA Trp ligase (AMP-forming), EC 6.1.1.2] from beef pancreas. The purification procedure comprises of five steps and yields about 130 mg of the enzyme per kilogram of tissue. The yield of the enzyme is considerably higher than that reported by others. Various properties and inhibitors of the given enzyme are described as well. From the mentioned data on beef pancreas tryptophanyl-tRNA synthetase it is concluded that this enzyme is characterized enzymologically rather intensively. Development of primary and three-dimensional structure investigations in the nearest future is expected because of the convenient and rapid procedure for enzyme purification. The availability of the specific inhibitors of different chemical nature makes it possible to evaluate various functional groups involved in the formation of active center. The mechanism of enzymic action needs to be investigated by means of fast kinetic methods.
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