Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver.

Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver. Research Abstract Details 

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Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver. Abstract Text:

T Nemoto,Y Ohara-Nemoto,M Ota,

The nontransformed glucocorticoid receptor (GR) and an 88-kDa protein in rat liver cytosol were selectively adsorbed on protamine- and arginine-Sepharose. The 88-kDa protein was purified from rat liver cytosol to homogeneity by precipitation with protamine sulfate, followed by DEAE-ion exchange chromatography, gel chromatography, and DEAE ion-exchange high-performance liquid chromatography. The 88-kDa protein appeared to be present as a dimer at both low and high salt concentrations. The physicochemical properties and the amino acid composition of the 88-kDa protein were almost the same as those of heat-shock protein 90 of HeLa cells and yeast. Preincubation of the GR with the polyclonal antibody raised against the 88-kDa protein increased the sedimentation coefficient of the nontransformed GR, but did not change that of the transformed GR. These results indicate that heat-shock protein 90 is associated with rat liver nontransformed GR and is responsible for the interaction of GR with protamine.

Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver. Publishing Authors By Initials

T Nemoto,Y Ohara-Nemoto,M Ota,

For similar organic chemicals: alcohols: fatty alcohols: dodecanol: sodium dodecyl sulfate research abstracts see: organic chemicals: alcohols: fatty alcohols: dodecanol: sodium dodecyl sulfate research

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Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 102

Page Numbers: 513-23

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1987

Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver. Keywords Mesh Terms:

KEYWORDS: Sodium Dodecyl Sulfate

MESH TERMS: metabolism

Chemical & Substance for Abstract: Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver. Information

Substance Name: Glycerol

Registry Number: 56-81-5

Grant and Affiliation Information for Purification and characterization of a nonhormone-binding component of the nontransformed glucocorticoid receptor from rat liver.

AFFILIATION: Department of Biochemistry, Iwate Medical University School of Dentistry.

Country: JAPAN

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MEDLINETA: J Biochem

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