Interaction of reduced glutathione with bovine brain tubulin

Asok Banerjee; Mary Ann Jordan; Richard F. Luduena

doi:10.1016/0006-291X(85)90075-0

Interaction of reduced glutathione with bovine brain tubulin

Asok Banerjee, Mary Ann Jordan, Richard F. Luduena

Department of Biochemistry & Structural Biology

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

7 Scopus citations

Abstract

Incubation of phosphocellulose-purified tubulin with GSH at 30°C results in an inhibition of colchicine binding activity. GSSG has a protective effect against the GSH-induced loss of colchicine-binding. Incubation of tubulin with GSH at 30°C results in the formation of abnormal tubulin polymers which are insensitive to cold. Such aggregation is insensitive to antimicrotubular drugs. Aggregation is inhibited by GSSG but not by DTT or mercaptoethanol. GSH-induced aggregation is very sensitive to the ionic strength of the assembly medium; both the aggregation and colchicine binding inhibition induced by GSH are inhibited at higher ionic strength. These results indicate a very complex interaction of GSH with tubulin.

Original language	English (US)
Pages (from-to)	506-512
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	128
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(85)90075-0
State	Published - Apr 30 1985

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Interaction of reduced glutathione with bovine brain tubulin",

abstract = "Incubation of phosphocellulose-purified tubulin with GSH at 30°C results in an inhibition of colchicine binding activity. GSSG has a protective effect against the GSH-induced loss of colchicine-binding. Incubation of tubulin with GSH at 30°C results in the formation of abnormal tubulin polymers which are insensitive to cold. Such aggregation is insensitive to antimicrotubular drugs. Aggregation is inhibited by GSSG but not by DTT or mercaptoethanol. GSH-induced aggregation is very sensitive to the ionic strength of the assembly medium; both the aggregation and colchicine binding inhibition induced by GSH are inhibited at higher ionic strength. These results indicate a very complex interaction of GSH with tubulin.",

author = "Asok Banerjee and Jordan, {Mary Ann} and Luduena, {Richard F.}",

note = "Funding Information: This study was supported and GM-23476 from National expert assistance of Phyllis is gratefully acknowledged.",

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T1 - Interaction of reduced glutathione with bovine brain tubulin

AU - Banerjee, Asok

AU - Jordan, Mary Ann

AU - Luduena, Richard F.

N1 - Funding Information: This study was supported and GM-23476 from National expert assistance of Phyllis is gratefully acknowledged.

PY - 1985/4/30

Y1 - 1985/4/30

N2 - Incubation of phosphocellulose-purified tubulin with GSH at 30°C results in an inhibition of colchicine binding activity. GSSG has a protective effect against the GSH-induced loss of colchicine-binding. Incubation of tubulin with GSH at 30°C results in the formation of abnormal tubulin polymers which are insensitive to cold. Such aggregation is insensitive to antimicrotubular drugs. Aggregation is inhibited by GSSG but not by DTT or mercaptoethanol. GSH-induced aggregation is very sensitive to the ionic strength of the assembly medium; both the aggregation and colchicine binding inhibition induced by GSH are inhibited at higher ionic strength. These results indicate a very complex interaction of GSH with tubulin.

AB - Incubation of phosphocellulose-purified tubulin with GSH at 30°C results in an inhibition of colchicine binding activity. GSSG has a protective effect against the GSH-induced loss of colchicine-binding. Incubation of tubulin with GSH at 30°C results in the formation of abnormal tubulin polymers which are insensitive to cold. Such aggregation is insensitive to antimicrotubular drugs. Aggregation is inhibited by GSSG but not by DTT or mercaptoethanol. GSH-induced aggregation is very sensitive to the ionic strength of the assembly medium; both the aggregation and colchicine binding inhibition induced by GSH are inhibited at higher ionic strength. These results indicate a very complex interaction of GSH with tubulin.

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Interaction of reduced glutathione with bovine brain tubulin

Abstract

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