1980Preparative BiochemistryRequires access

Purification of Low Molecular Weight Metal-Binding Proteins by Preparative Polyacrylamide Gel Electrophoresis: Properties of Electrophoretically Purified Rat Liver (Cd, Zn)-Metallothioneins

Andrzej J. Żelazowski, Jadwiga A. Szymańska, Henryk W. Witas

Open publisher page 28 citations

Abstract

A method is proposed for purification of metallothionein by preparative polyacrylamide gel electrophoresis. The method enables purification of 100-700 mg of a preparation containing (Cd, Zn) - metallothionein yielding preparations of considerably higher purity as compared with those obtained by ion-exchange chromatography.

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A method is proposed for purification of metallothionein by preparative polyacrylamide gel electrophoresis. The method enables purification of 100-700 mg of a preparation containing (Cd, Zn) - metallothionein yielding preparations of considerably higher purity as compared with those obtained by ion-exchange chromatography.

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Available abstract

A method is proposed for purification of metallothionein by preparative polyacrylamide gel electrophoresis. The method enables purification of 100-700 mg of a preparation containing (Cd, Zn) - metallothionein yielding preparations of considerably higher purity as compared with those obtained by ion-exchange chromatography.

Key concepts: Metallothionein, Polyacrylamide gel electrophoresis, Chromatography, Chemistry, Polyacrylamide, Electrophoresis, Gel electrophoresis, Gel electrophoresis of proteins

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Purification of Low Molecular Weight Metal-Binding Proteins by Preparative Polyacrylamide Gel Electrophoresis: Properties of Electrophoretically Purified Rat Liver (Cd, Zn)-Metallothioneins — Research Paper | ScholarLens