Purification of pseudouridylate synthetase I from Salmonella typhimurium | Zendy

Francesco Arena | Zendy; Gennaro Ciliberto | Zendy; Sofia Ciampi | Zendy; Riccardo Cortese | Zendy

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Purification of pseudouridylate synthetase I from Salmonella typhimurium

Author(s) -

Francesco Arena,

Gennaro Ciliberto,

Sofia Ciampi,

Riccardo Cortese

Publication year - 1978

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/5.12.4523

Subject(s) - biology , enzyme , salmonella , transfer rna , biochemistry , enterobacteriaceae , bacteria , microbiology and biotechnology , escherichia coli , genetics , rna , gene

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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