DOI: 10.1073/pnas.83.16.5904. Affinity chromatography with an immobilized RNA enzyme.

Affinity chromatography with an immobilized RNA enzyme.

10.1073/pnas.83.16.5904

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

M1 RNA, the catalytic subunit of Escherichia coli RNase P, has been covalently linked at its 3' terminus to agarose beads. Unlike M1 RNA, which is active in solution in the absence of the protein component (C5) of RNase P, the RNA linked to the beads is active only in the presence of C5 protein. Affinity chromatography of crude extracts of E. coli on a column prepared from the beads to which the RNA has been crosslinked results in the purification of C5 protein in a single step. The protein has been purified in this manner from cells that contain a plasmid, pINIIIR20, which includes the gene that codes for C5 protein. A 6-fold amplification of the expression of C5 protein is found in these cells after induction as compared to cells that do not harbor the plasmid.

Bibliography

Vioque, A., & Altman, S. (1986). Affinity chromatography with an immobilized RNA enzyme. Proceedings of the National Academy of Sciences, 83(16), 5904â5908.

Authors 2

A Vioque (first)
S Altman (additional)

References 0 Referenced 25

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 6:02 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 12:19 p.m.)
Indexed	1 year, 1 month ago (Aug. 4, 2024, 2:34 p.m.)
Issued	39 years, 1 month ago (Aug. 1, 1986)
Published	39 years, 1 month ago (Aug. 1, 1986)
Published Online	39 years, 1 month ago (Aug. 1, 1986)
Published Print	39 years, 1 month ago (Aug. 1, 1986)

Funders 0

None

BibTeX

@article{Vioque_1986, title={Affinity chromatography with an immobilized RNA enzyme.}, volume={83}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.83.16.5904}, DOI={10.1073/pnas.83.16.5904}, number={16}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Vioque, A and Altman, S}, year={1986}, month=aug, pages={5904–5908} }

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