Effect of 2-mercaptoethanol on the electrophoretic behavior of rat and dogfish metallothionein and chromatographic evidence of a naturally occurring metallothionein polymerization

Juan Hidalgo; Jordi Bernues; Dafydd G. Thomas; Justine S. Garvey

doi:10.1016/0742-8413(88)90208-3

Effect of 2-mercaptoethanol on the electrophoretic behavior of rat and dogfish metallothionein and chromatographic evidence of a naturally occurring metallothionein polymerization

Juan Hidalgo^*, Jordi Bernues, Dafydd G. Thomas, Justine S. Garvey

^*Corresponding author for this work

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

22 Citations (Scopus)

Abstract

1. Metallothionein behavior in SDS-PAGE has been characterized. 2. It has been found that metallothionein behavior in this electrophoretic system depends upon the reducing environment. Migration as a well-defined protein band is only achieved in the presence of 2-100 mM 2-mercaptoethanol. 3. Within those 2-mercaptoethanol levels, both rat and dogfish metallothionein migrate as a protein with a molecular weight several times higher than that expected by amino acid analyses. This is not due to molecule oxidations, since this effect is promoted by the presence of 2-mercaptoethanol. 4. No effect of 2-mercaptoethanol on metallothionein behavior is found in conventional PAGE. 5. The present results suggest that to study the effect of 2-mercaptoethanol in SDS-PAGE is a simple and accurate way to identify a protein as metallothionein. 6. It has also been found that metallothionein aggregates naturally in the absence of ionic strength. © 1988.

Original language	English
Pages (from-to)	191-196
Journal	Comparative Biochemistry and Physiology. Part C, Comparative
Volume	89
Issue number	2
DOIs	https://doi.org/10.1016/0742-8413(88)90208-3
Publication status	Published - 1 Jan 1988

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@article{aa9b7a38bb3942f19225ed866c533db3,

title = "Effect of 2-mercaptoethanol on the electrophoretic behavior of rat and dogfish metallothionein and chromatographic evidence of a naturally occurring metallothionein polymerization",

abstract = "1. Metallothionein behavior in SDS-PAGE has been characterized. 2. It has been found that metallothionein behavior in this electrophoretic system depends upon the reducing environment. Migration as a well-defined protein band is only achieved in the presence of 2-100 mM 2-mercaptoethanol. 3. Within those 2-mercaptoethanol levels, both rat and dogfish metallothionein migrate as a protein with a molecular weight several times higher than that expected by amino acid analyses. This is not due to molecule oxidations, since this effect is promoted by the presence of 2-mercaptoethanol. 4. No effect of 2-mercaptoethanol on metallothionein behavior is found in conventional PAGE. 5. The present results suggest that to study the effect of 2-mercaptoethanol in SDS-PAGE is a simple and accurate way to identify a protein as metallothionein. 6. It has also been found that metallothionein aggregates naturally in the absence of ionic strength. {\textcopyright} 1988.",

author = "Juan Hidalgo and Jordi Bernues and Thomas, {Dafydd G.} and Garvey, {Justine S.}",

year = "1988",

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day = "1",

doi = "10.1016/0742-8413(88)90208-3",

language = "English",

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pages = "191--196",

number = "2",

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Hidalgo, J, Bernues, J, Thomas, DG & Garvey, JS 1988, 'Effect of 2-mercaptoethanol on the electrophoretic behavior of rat and dogfish metallothionein and chromatographic evidence of a naturally occurring metallothionein polymerization', Comparative Biochemistry and Physiology. Part C, Comparative, vol. 89, no. 2, pp. 191-196. https://doi.org/10.1016/0742-8413(88)90208-3

Effect of 2-mercaptoethanol on the electrophoretic behavior of rat and dogfish metallothionein and chromatographic evidence of a naturally occurring metallothionein polymerization. / Hidalgo, Juan; Bernues, Jordi; Thomas, Dafydd G.; Garvey, Justine S.

In: Comparative Biochemistry and Physiology. Part C, Comparative, Vol. 89, No. 2, 01.01.1988, p. 191-196.

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

TY - JOUR

T1 - Effect of 2-mercaptoethanol on the electrophoretic behavior of rat and dogfish metallothionein and chromatographic evidence of a naturally occurring metallothionein polymerization

AU - Hidalgo, Juan

AU - Bernues, Jordi

AU - Thomas, Dafydd G.

AU - Garvey, Justine S.

PY - 1988/1/1

Y1 - 1988/1/1

N2 - 1. Metallothionein behavior in SDS-PAGE has been characterized. 2. It has been found that metallothionein behavior in this electrophoretic system depends upon the reducing environment. Migration as a well-defined protein band is only achieved in the presence of 2-100 mM 2-mercaptoethanol. 3. Within those 2-mercaptoethanol levels, both rat and dogfish metallothionein migrate as a protein with a molecular weight several times higher than that expected by amino acid analyses. This is not due to molecule oxidations, since this effect is promoted by the presence of 2-mercaptoethanol. 4. No effect of 2-mercaptoethanol on metallothionein behavior is found in conventional PAGE. 5. The present results suggest that to study the effect of 2-mercaptoethanol in SDS-PAGE is a simple and accurate way to identify a protein as metallothionein. 6. It has also been found that metallothionein aggregates naturally in the absence of ionic strength. © 1988.

AB - 1. Metallothionein behavior in SDS-PAGE has been characterized. 2. It has been found that metallothionein behavior in this electrophoretic system depends upon the reducing environment. Migration as a well-defined protein band is only achieved in the presence of 2-100 mM 2-mercaptoethanol. 3. Within those 2-mercaptoethanol levels, both rat and dogfish metallothionein migrate as a protein with a molecular weight several times higher than that expected by amino acid analyses. This is not due to molecule oxidations, since this effect is promoted by the presence of 2-mercaptoethanol. 4. No effect of 2-mercaptoethanol on metallothionein behavior is found in conventional PAGE. 5. The present results suggest that to study the effect of 2-mercaptoethanol in SDS-PAGE is a simple and accurate way to identify a protein as metallothionein. 6. It has also been found that metallothionein aggregates naturally in the absence of ionic strength. © 1988.

U2 - 10.1016/0742-8413(88)90208-3

DO - 10.1016/0742-8413(88)90208-3

M3 - Article

VL - 89

SP - 191

EP - 196

IS - 2

ER -