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[Analysis of cerebellar proteins and glycoproteins in adult cattle. I. Con A positive glycoproteins].

D Ruccia, Gianfranco Gennarini, Patrizia Corsi, Di Benedetta C

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Abstract

The cerebellar glycoproteins of bovine have been separated by affinity chromatography on Con A-Sepharose and analyzed by poliacrylamide gel electrophoresis. Some soluble Con A binding glycoproteins are common to the insoluble (membrane bound) glycoproteins suggesting a relationship between the two classes of molecules. The data support the hypothesis that some of the soluble glycoproteins can be considered precursors of the insoluble.

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The cerebellar glycoproteins of bovine have been separated by affinity chromatography on Con A-Sepharose and analyzed by poliacrylamide gel electrophoresis. Some soluble Con A binding glycoproteins are common to the insoluble (membrane bound) glycoproteins suggesting a relationship between the two classes of molecules. The data support the hypothesis that some of the soluble glycoproteins can be considered precursors of the insoluble.

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Available abstract

The cerebellar glycoproteins of bovine have been separated by affinity chromatography on Con A-Sepharose and analyzed by poliacrylamide gel electrophoresis. Some soluble Con A binding glycoproteins are common to the insoluble (membrane bound) glycoproteins suggesting a relationship between the two classes of molecules. The data support the hypothesis that some of the soluble glycoproteins can be considered precursors of the insoluble.

Key concepts: Glycoprotein, Membrane glycoproteins, Biochemistry, Chemistry, Electrophoresis, Affinity chromatography, Gel electrophoresis, Enzyme

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[Analysis of cerebellar proteins and glycoproteins in adult cattle. I. Con A positive glycoproteins]. — Research Paper | ScholarLens