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

ASJC Scopus subject areas

General Medicine

Access to Document

10.1016/0005-2787(75)90099-4

Cite this

@article{7a8f99f38d854ba9938ac61ca339870d,

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).",

year = "1975",

month = oct,

day = "15",

doi = "10.1016/0005-2787(75)90099-4",

language = "English (US)",

volume = "407",

pages = "320--324",

journal = "BBA Section Nucleic Acids And Protein Synthesis",

issn = "0005-2787",

publisher = "Elsevier BV",

number = "3",

}

TY - JOUR

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.

UR - http://www.scopus.com/inward/record.url?scp=0016720298&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016720298&partnerID=8YFLogxK

U2 - 10.1016/0005-2787(75)90099-4

DO - 10.1016/0005-2787(75)90099-4

M3 - Article

C2 - 1102783

AN - SCOPUS:0016720298

SN - 0005-2787

VL - 407

SP - 320

EP - 324

JO - BBA Section Nucleic Acids And Protein Synthesis

JF - BBA Section Nucleic Acids And Protein Synthesis

IS - 3

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this