Phosphorylation of a nonhistone protein fraction which coextracts with the high-mobility-group proteins of chromatin

Khalil Ahmed; Alan T. Davis; Said A. Goueli; Michael J. Wilson

doi:10.1016/0006-291X(80)91218-8

Phosphorylation of a nonhistone protein fraction which coextracts with the high-mobility-group proteins of chromatin

Khalil Ahmed, Alan T. Davis, Said A. Goueli, Michael J. Wilson

Laboratory Medicine and Pathology

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

7 Scopus citations

Abstract

³²P-labelled chromatin proteins from rat liver and ventral prostate were fractionated according to the procedure designed to enrich high-mobility-group (HMG) nonhistone proteins. This fraction, however, reproducibly demonstrated small amounts of apparently basic nonhistone proteins other than HMG nonhistone proteins. These proteins appeared to be tissue specific and were highly labelled with ³²P. The ³²P-labelled phosphoproteins were soluble in trichloroacetic or perchloric acid, migrated in acid-urea polyacrylamide gels, and demonstrated pI values ranging from 6.8 to 7.5. The HMG proteins 1 and 2 showed no incorporation of radioactivity under these experimental conditions.

Original language	English (US)
Pages (from-to)	326-332
Number of pages	7
Journal	Topics in Catalysis
Volume	96
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(80)91218-8
State	Published - 1980

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title = "Phosphorylation of a nonhistone protein fraction which coextracts with the high-mobility-group proteins of chromatin",

abstract = "32P-labelled chromatin proteins from rat liver and ventral prostate were fractionated according to the procedure designed to enrich high-mobility-group (HMG) nonhistone proteins. This fraction, however, reproducibly demonstrated small amounts of apparently basic nonhistone proteins other than HMG nonhistone proteins. These proteins appeared to be tissue specific and were highly labelled with 32P. The 32P-labelled phosphoproteins were soluble in trichloroacetic or perchloric acid, migrated in acid-urea polyacrylamide gels, and demonstrated pI values ranging from 6.8 to 7.5. The HMG proteins 1 and 2 showed no incorporation of radioactivity under these experimental conditions.",

author = "Khalil Ahmed and Davis, {Alan T.} and Goueli, {Said A.} and Wilson, {Michael J.}",

year = "1980",

doi = "10.1016/0006-291X(80)91218-8",

language = "English (US)",

volume = "96",

pages = "326--332",

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T1 - Phosphorylation of a nonhistone protein fraction which coextracts with the high-mobility-group proteins of chromatin

AU - Ahmed, Khalil

AU - Davis, Alan T.

AU - Goueli, Said A.

AU - Wilson, Michael J.

PY - 1980

Y1 - 1980

N2 - 32P-labelled chromatin proteins from rat liver and ventral prostate were fractionated according to the procedure designed to enrich high-mobility-group (HMG) nonhistone proteins. This fraction, however, reproducibly demonstrated small amounts of apparently basic nonhistone proteins other than HMG nonhistone proteins. These proteins appeared to be tissue specific and were highly labelled with 32P. The 32P-labelled phosphoproteins were soluble in trichloroacetic or perchloric acid, migrated in acid-urea polyacrylamide gels, and demonstrated pI values ranging from 6.8 to 7.5. The HMG proteins 1 and 2 showed no incorporation of radioactivity under these experimental conditions.

AB - 32P-labelled chromatin proteins from rat liver and ventral prostate were fractionated according to the procedure designed to enrich high-mobility-group (HMG) nonhistone proteins. This fraction, however, reproducibly demonstrated small amounts of apparently basic nonhistone proteins other than HMG nonhistone proteins. These proteins appeared to be tissue specific and were highly labelled with 32P. The 32P-labelled phosphoproteins were soluble in trichloroacetic or perchloric acid, migrated in acid-urea polyacrylamide gels, and demonstrated pI values ranging from 6.8 to 7.5. The HMG proteins 1 and 2 showed no incorporation of radioactivity under these experimental conditions.

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Phosphorylation of a nonhistone protein fraction which coextracts with the high-mobility-group proteins of chromatin

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