ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Abstract— The activity and kinetic characteristics of tRNA methyltransferases were measured with enzyme preparations obtained from neonatal and adult mouse brain tissue. Both neonatal and mature brain enzyme preparations were shown to contain a considerable amount of protein methylase activity which could interfere with the measurement of the tRNA methyltransferases. When increasing amounts of the unfractionated enzymes from young and adult neural tissue were added to reaction mixtures, the saturation kinetics were found to be considerably different. However, fractionation of the samples by precipitation at pH 5 resulted in an increase in the enzyme activity of preparations obtained from adult brain. Although the precipitation at pH 5 allowed a quantitative recovery of the enzyme activity of immature brain samples, this partial purification step led to an apparent activation of the tRNA methyltransferases in adult preparations. This activation was shown to be independent of differential changes in the thermolability of the enzymes but rather to be associated with an increase in the sites methylated and the measured affinity of the adult enzyme preparations with the tRNA substrate. Nicotinamide, a potent inhibitor of tRNA methyltransferase activity in other tissues, was shown to be ineffective in modulating brain tRNA methyltransferase activity. The results are discussed in light of the possible modulation of the activity of specific enzyme species and the alterations in the synthesis of nucleic acid precursors during neural development.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1471-4159.1974.tb06050.x
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