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. 1978 Dec;5(12):4523–4536. doi: 10.1093/nar/5.12.4523

Purification of pseudouridylate synthetase I from Salmonella typhimurium.

F Arena, G Ciliberto, S Ciampi, R Cortese
PMCID: PMC342770  PMID: 370771

Abstract

Pseudouridylate synthetase from Salmonella typhimurium has been purified 1,000 fold and is about 90% pure. The enzyme has a molecular weight of 50,000 daltons. In the presence of tRNA there is a change in molecular weight from 50.000 to 100.000. This change does not seem to be due to the formation of a tRNA-enzyme complex but rather to a tRNA induced dimerization. Other properties of the enzyme are described.

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Selected References

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