Characterization of the particles produced by exposure of ribosomal subunits to urea

J. A. Langer; A. S. Acharya; P. B. Moore

doi:10.1016/0005-2787(75)90099-4

Characterization of the particles produced by exposure of ribosomal subunits to urea

J. A. Langer, A. S. Acharya, P. B. Moore

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

When Escherichia coli 50-S ribosomal subunits are treated with increasing concentrations of urea partial deproteination occurs. Furthermore, we observed that the number of sulfhydryl groups which react with Ellman's reagent is a sigmoidal function of the urea concentration. These results are similar to those previously reported for the 30-S subunit (Acharya, A.S. and Moore, P.B. (1973) J. Mol. Biol. 76, 207-221). For both subunits we identify the proteins which dissociate (split proteins) or are recoverable in a ribonucleoprotein particle (core proteins) under the action of 6 M urea in a buffer of moderate ionic strength.

Original language	English (US)
Pages (from-to)	320-324
Number of pages	5
Journal	BBA Section Nucleic Acids And Protein Synthesis
Volume	407
Issue number	3
DOIs	https://doi.org/10.1016/0005-2787(75)90099-4
State	Published - Oct 15 1975
Externally published	Yes

All Science Journal Classification (ASJC) codes

General Medicine

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10.1016/0005-2787(75)90099-4

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title = "Characterization of the particles produced by exposure of ribosomal subunits to urea",

abstract = "When Escherichia coli 50-S ribosomal subunits are treated with increasing concentrations of urea partial deproteination occurs. Furthermore, we observed that the number of sulfhydryl groups which react with Ellman's reagent is a sigmoidal function of the urea concentration. These results are similar to those previously reported for the 30-S subunit (Acharya, A.S. and Moore, P.B. (1973) J. Mol. Biol. 76, 207-221). For both subunits we identify the proteins which dissociate (split proteins) or are recoverable in a ribonucleoprotein particle (core proteins) under the action of 6 M urea in a buffer of moderate ionic strength.",

author = "Langer, {J. A.} and Acharya, {A. S.} and Moore, {P. B.}",

note = "Funding Information: This work was supported by a grant from the National Institutes of Health (AI-09167).",

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T1 - Characterization of the particles produced by exposure of ribosomal subunits to urea

AU - Langer, J. A.

AU - Acharya, A. S.

AU - Moore, P. B.

N1 - Funding Information: This work was supported by a grant from the National Institutes of Health (AI-09167).

PY - 1975/10/15

Y1 - 1975/10/15

N2 - When Escherichia coli 50-S ribosomal subunits are treated with increasing concentrations of urea partial deproteination occurs. Furthermore, we observed that the number of sulfhydryl groups which react with Ellman's reagent is a sigmoidal function of the urea concentration. These results are similar to those previously reported for the 30-S subunit (Acharya, A.S. and Moore, P.B. (1973) J. Mol. Biol. 76, 207-221). For both subunits we identify the proteins which dissociate (split proteins) or are recoverable in a ribonucleoprotein particle (core proteins) under the action of 6 M urea in a buffer of moderate ionic strength.

AB - When Escherichia coli 50-S ribosomal subunits are treated with increasing concentrations of urea partial deproteination occurs. Furthermore, we observed that the number of sulfhydryl groups which react with Ellman's reagent is a sigmoidal function of the urea concentration. These results are similar to those previously reported for the 30-S subunit (Acharya, A.S. and Moore, P.B. (1973) J. Mol. Biol. 76, 207-221). For both subunits we identify the proteins which dissociate (split proteins) or are recoverable in a ribonucleoprotein particle (core proteins) under the action of 6 M urea in a buffer of moderate ionic strength.

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Characterization of the particles produced by exposure of ribosomal subunits to urea

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