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Electroblot analysis of the myelin proteolipid protein

Wendy B. Macklin, Peter E. Braun, Marjorie B. Lees

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Abstract

The myelin proteolipid has been studied by the electroblot method of Towbin et al [1979]. Samples were separated by SDS-polyacrylamide gel electrophoresis, transferred to nitrocellulose, and incubated with proteolipid antibody. The proteolipid band could be identified immunologically in CNS myelin and in whole brain homogenates. No proteolipid was detected in PNS myelin. Proteolipid from human, bovine, rat, and mouse myelin all cross-react when analyzed by this method. No cross-reactivity was indicated between proteolipid and myelin basic protein.

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What this paper is about

The myelin proteolipid has been studied by the electroblot method of Towbin et al [1979]. Samples were separated by SDS-polyacrylamide gel electrophoresis, transferred to nitrocellulose, and incubated with proteolipid antibody. The proteolipid band could be identified immunologically in CNS myelin and in whole brain homogenates. No proteolipid was detected in PNS myelin. Proteolipid from human, bovine, rat, and mouse myelin all cross-react when analyzed by this method. No cross-reactivity was indicated between proteolipid and myelin basic protein.

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Available abstract

The myelin proteolipid has been studied by the electroblot method of Towbin et al [1979]. Samples were separated by SDS-polyacrylamide gel electrophoresis, transferred to nitrocellulose, and incubated with proteolipid antibody. The proteolipid band could be identified immunologically in CNS myelin and in whole brain homogenates. No proteolipid was detected in PNS myelin. Proteolipid from human, bovine, rat, and mouse myelin all cross-react when analyzed by this method. No cross-reactivity was indicated between proteolipid and myelin basic protein.

Key concepts: Myelin, Proteolipid protein 1, Myelin proteolipid protein, Nitrocellulose, Polyacrylamide gel electrophoresis, Chemistry, Myelin basic protein, Biochemistry

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