Dogfish metallothionein-II. Electrophoretic studies and comparison with rat metallothionein

Juan Hidalgo; Rosa Flos

doi:10.1016/0742-8413(86)90020-4

Dogfish metallothionein-II. Electrophoretic studies and comparison with rat metallothionein

Juan Hidalgo^*, Rosa Flos

^*Corresponding author for this work

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

11 Citations (Scopus)

Abstract

1. 1. A low-molecular weight metal-binding protein has been isolated and characterized as metallothionein in the liver of the dogfish (Scyliorhinus canicula). 2. 2. This protein is present in both male and female animals and both control and cadmium-treated (both water and i.p. administration) animals as revealed by SDS-PAGE studies. 3. 3. Dogfish metallothionein shows the same metal-dependent anomalous behaviour as rat metallothionein in SDS-PAGE. 4. 4. SDS-PAGE is a good method to identify a protein as metallothionein. © 1986.

Original language	English
Pages (from-to)	105-109
Journal	Comparative Biochemistry and Physiology. Part C, Comparative
Volume	83
Issue number	1
DOIs	https://doi.org/10.1016/0742-8413(86)90020-4
Publication status	Published - 1 Jan 1986

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title = "Dogfish metallothionein-II. Electrophoretic studies and comparison with rat metallothionein",

abstract = "1. 1. A low-molecular weight metal-binding protein has been isolated and characterized as metallothionein in the liver of the dogfish (Scyliorhinus canicula). 2. 2. This protein is present in both male and female animals and both control and cadmium-treated (both water and i.p. administration) animals as revealed by SDS-PAGE studies. 3. 3. Dogfish metallothionein shows the same metal-dependent anomalous behaviour as rat metallothionein in SDS-PAGE. 4. 4. SDS-PAGE is a good method to identify a protein as metallothionein. {\textcopyright} 1986.",

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N2 - 1. 1. A low-molecular weight metal-binding protein has been isolated and characterized as metallothionein in the liver of the dogfish (Scyliorhinus canicula). 2. 2. This protein is present in both male and female animals and both control and cadmium-treated (both water and i.p. administration) animals as revealed by SDS-PAGE studies. 3. 3. Dogfish metallothionein shows the same metal-dependent anomalous behaviour as rat metallothionein in SDS-PAGE. 4. 4. SDS-PAGE is a good method to identify a protein as metallothionein. © 1986.

AB - 1. 1. A low-molecular weight metal-binding protein has been isolated and characterized as metallothionein in the liver of the dogfish (Scyliorhinus canicula). 2. 2. This protein is present in both male and female animals and both control and cadmium-treated (both water and i.p. administration) animals as revealed by SDS-PAGE studies. 3. 3. Dogfish metallothionein shows the same metal-dependent anomalous behaviour as rat metallothionein in SDS-PAGE. 4. 4. SDS-PAGE is a good method to identify a protein as metallothionein. © 1986.

U2 - 10.1016/0742-8413(86)90020-4

DO - 10.1016/0742-8413(86)90020-4

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